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 Capping 1 modified guanosine nucleotide / 7-methylguanosine / added to 5’ end of mRNA; 2 enzymes (e.g. guanyl / methyl transferase) catalyses reaction between 5’ end of the RNA transcript and GTP; 3 ref. association of cap-binding protein Polyadenylation 4 addition of 30-200 adenine sequences to the 3’ end of the pre-mRNA; 5 after polyadenylation signal has been transcribed; 6 catalysed by poly(A) polymerase / polyadenylate polymerase; 7 ref. poly-A binding protein binds to poly(A) tail Splicing 8 Splicing is catalyzed by snRNPs / small nuclear ribonucleoproteins 9 snRNPs are made up of proteins & snRNA (small nuclear RNA) 10 snRNPs + other proteins join together to form a complex called spliceosomes 11 spliceosomes is first responsible for folding the pre-mRNA into the correct orientation for splicing 12 splicing involves cleavage of the 5’ end of the intron 13 and its attachment to the branchpoint sequence 14 to form a tailed loop structure called a lariat 15 intron is then excised/released 16 by being cleaved at its 3’ end 17 and the exons are brought together and ligated 18 spliceosomes dissociates once splicing is completed 8(b) Compare structure and organisation of prokaryotic and eukaryotic chromosome.  [½ mark per correct comparison] Prokayotic genome Eukaryotic genome 1. Genome size Smaller genomes, 0.6 to 10Mb. Large genomes, being less than 10 Mb – 100,000 Mb 2. Gene length Shorter gene sequences / more compact genetic organisation Longer gene sequences / presence of more intergenic spaces 3. Chromosome number Single chromosome / Haploid Many chromosomes / Diploid or polyploid 4. Chromosome structure Circular DNA molecule. Linear DNA, each contained in a different chromosome. 5. Location Chromosome found in the nucleoid region of the cytoplasm Chromosomes are enclosed within a double-membrane bound nucleus 6. Packaging of DNA Does not form chromatin. (Prokaryotic DNA is organized into a DNA-protein complex called the nucleoid. Eukaryotic DNA is complexed with histones and other proteins to form chromatin. 7. Introns Coding sequence proceeds from start to finish without interruption by introns. Presence of introns within genes. 8. Repetitive sequences Few repetitive DNA sequences. Many highly repetitive DNA sequences
9. Coding and non-coding DNA Most of DNA are coding sequences (codes for protein, tRNA, or rRNA. Most of DNA are noncoding. 10. Regulatory sequences Small amount of non-coding DNA consists mainly of regulatory sequences, such as promoters) More complex regulatory sequences (eg. enhancers and silencers) 11. Presence and absence of operons Two or more genes may be expressed and regulated as a unit (genomes arranged in operons / polycistronic genes) Absence of operons / monocistronic genes 12. Origins of replication One Many 13. Presence of extrachromosomal DNA Independent small, circular, molecules called plasmids. Circular, double-stranded DNA in mitochondria / choloroplasts. 14. Telomeres Absent Present 15. Centromere Absent Present
8(c) Outline the differences between prokaryotic control of gene expression with the eukaryotic model.  For every comparison: ½ mark for correct comparison ½ mark for correct information Chromosomal Level (max 2) Prokaryotes Eukaryotes 1. DNA and histone modification cannot occur (Prokaryotic DNA does not form chromatin / not associated with histones) DNA and histone modification can occur, resulting in conversion between euchromatin and heterochromatin, and hence the ease of transcription (Eukaryotic DNA is complexed with histones and other proteins to form chromatin / associated with histones) 2. DNA sequences, including operators and activators, serve as the on/off switch Structure of chromatin – euchromatin, ready to be transcribed, or heterochromatin and not available – is the major on/off switch for gene regulation 3. Prokaryotic DNA not organised into chromatin. Initiation of transcription of eukaryotic genes requires that the compact chromatin fibre, characterised by nucleosome coiling, to be uncoiled and the DNA made accessible to RNA polymerase and other regulatory proteins. Transcriptional Level (max 2) Prokaryotes Eukaryotes 4. One RNA polymerase consisting of five subunits / All RNAs synthesized by the same RNA polymerase;
Occurs within the nucleus under the direction of three separate forms of RNA polymerases, each containing 10 or more subunits; different polymerases transcribe different genes / Three different classes of RNA each synthesized by a different RNA polymerase 5. Simple regulatory sequence: Transcriptional regulatory protein / Regulator protein binds to DNA-binding sites upstream of the cluster of structural genes to regulate initiation of transcription. Complex regulatory sequence: More extensive interaction between upstream DNA sequences and protein factors involved to stimulate and initiate transcription. In addition to promoters, enhancers and silencers control rate of transcription initiation 6. Related genes are transcribed together as operons / only 1 promoter / polycistronic mRNA
No operon / each gene has own promoter / monocistronic mRNA Post-transcriptional Level (max 2) Prokaryotes Eukaryotes 7. no/minimal post-translational modifications occur Post-translational modifications determine the functional abilities of the protein . Triphosphate start at the 5’ end / No tail at the 3’ end / No splicing Methylated guanosine cap at the 5’ end / Poly-A tail at the 3’ end / Splicing occurs (also alternative splicing) 10. Small ribosomal subunit immediately binds to the mRNA’s ribosome binding site Small ribosomal subunits bind first to the methylated cap at the 5’ end of the mature mRNA and then scans the mRNA to find the ribosome binding site. 8. RNA transcript is not free to associate with ribosomes prior to the completion of transcription). Unique initiator tRNA carries formylmethionine Initiator tRNA carries methionine 13. Control at this level is unlikely. mRNAs have multiple ribosome binding sites / direct the synthesis of several different polypeptides mRNAs have only one start site / direct synthesis of only one kind of polypeptide 15. Lower stability of transcript / degradation within seconds or minutes / mRNAs shorter half life to rapidly respond to environmental changes Higher stability of transcript / prevent transcript degradation / mRNAs longer half-life remaining much longer to orchestrate protein synthesis prior to their degradation by nucleases in the cell Translational level (max 2) Prokaryotes Eukaryotes 11. Translation is often coupled to transcription (Transcription and translation take place in the same cellular compartment simultaneously) No direct coupling of transcription and translation. the AUG start codon Post-translational Level (max 2) Prokaryotes Eukaryotes 16. (mRNA must pass across nuclear envelope before translation in the cytoplasm. Smaller ribosomes / less complex rRNA and protein components Occurs on ribosomes that are larger / rRNA and protein components are more complex than those of prokaryotes 14. due to simultaneous transcription and translation Control at translational level: phosphorylation of ribosomal translation initiation factors / negative translational control through regulatory proteins / cytoplasmic elongation of poly (A) tails / mRNA degradation / RNA interference and microRNA 12. Primary transcripts are the actual mRNAs /no post-transcriptional modification Primary transcripts undergo processing to produce mature mRNAs / post-transcriptional modification 9.
replication of viral genome 15 metabolically inert / do not grow or divide on their own 16 can only multiply inside living cells. herpes virus etc 2 animal viruses composed of phospholipids/glycoprotein envelope 3 similar in nature to cell surface membrane of animal cell 4 with glycoprotein spikes (for attachment to host cell membrane) 5 enclosed in the viral envelope is the capsid 6 which is composed of capsomeres / protein subunits 7 which contains the viral genome 8 either DNA or RNA.g. signal sequence is enzymatically removed from the proteins 21. and explain why viruses are obligate parasites. penetration. Ubiquitination marks protein for degradation. and release 2 Both attach to their host cell at receptor sites on the host cell’s plasma membrane.17. antigenic drift 2 8 single-stranded RNA segments 3 spontaneous genetic mutation /mutation during replication 4 lack of proof-reading during RNA replication 5 ref. HIV. Chemical modification of proteins to yield functional protein molecules 19. Transportation of proteins to target destinations in the cell where it functions is mediated by signal sequences at N-terminus of some proteins. ref to ubiquitin & proteasome 9(a) Describe the general structure of a named animal virus. cleavage of pro-insulin to form the active insulin hormone 18. viral enzymes (eg. replication. Proteolysis: Processing eukaryotic polypeptides to yield functional protein molecules e. etc 10 ref. antigenic shift 6 genetic reassortment of the RNA segments between two strains of viruses 7 novel glycoproteins (spikes) produced on viral envelope /modified neuraminidase and haemaglutinin 8 cannot be recognized by previous antibodies 9(c) Compare and contrast the reproductive cycles of the Lambda phage and the Human Immunodeficiency Virus (HIV). Phosphorylation of proteins to increase or decrease its function 20. and not on inanimate media 9(b) Outline how the influenza virus is able to bypass the human defense mechanism to cause disease. linear or circular.  1 ref.  1 example of animal viruses: influzena. reverse transcriptase in HIV) 11 acellular / absence of cytoplasm and cellular organelles 12 lacks ribosomes / protein-synthesising apparatus 13 hijacks host cell’s host’s protein synthesis machinery (transcription and translation machineries) to produce own viral proteins [REJECT ‘metabolic machinery’] 14 ref.  [1 mark per similarity] (max 4) 1 Life cycle of both viruses involves the stages attachment. maturation. single-stranded or double-stranded. Once transported to destination. 3 Both introduce their viral nucleic acids into their host cell 4 Both are obligate intracellular parasites/make use of their host cell’s resources for synthesis of viral proteins and nucleic acids 5 Both integrate their viral DNA into host genome/viral DNA replicates as part of host’s DNA every time the cell divides [1 mark per difference] (max 6) Feature of comparison Lambda phage HIV . but never both 9 either single or segmented.
breakdown of glycogen to glucose. HIV envelope fuses with the host cell’s plasma membrane. 5. effects of glucagon are antagonistic to insulin. Uncoating 9 No uncoating required as capsid does not enter host cell. T4 phages attach to specific surface structures called receptor sites. As more tail fibres make contact. 6. 11 Can enter lytic phase or lysogenic phrase (prophage). . Bacteriophages do not randomly attach to the surface of a host cell. 12 Prophage is excised from host cell’s chromosome upon spontaneous induction. 8 Phage injects only its ds DNA. using a named example. 7. conformation changes occur in the baseplate and sheath. the phage tail pins attach via strong interaction to receptor (outer membrane proteins) on surface of outer membrane of host cell. Viral genome incorporated into host cell chromosomes (provirus). 2.  1. Provirus is not excised as viral mRNA is transcribed from viral DNA together with host cell’s genes. liver releases glucose into blood and glucose levels rise and return to normal at 90mg/100ml. Fate of viral nucleic acids 10 No reverse transcription / ds DNA is either immediately used as template for synthesis of viral proteins and nucleic acids (lytic cycle) or integrated into bacterial chromosome. Specific strains of bacteriophages can only adsorb to specific strain of host bacteria. glucagon released from alpha cells in pancreas which acts on liver cells. when blood glucose levels low. The new viruses bud off from host cell’s plasma membrane. They use cell wall lipopolysaccharides or proteins as receptors. Release / Exit 14 Host cell is lysed to release the new viruses. production of glucose from other compounds / fats / amino acids / via gluconeogenesis. Sheath contracts and tail tube penetrates outer membrane. this is known as viral specificity. using reverse transcriptase. 3. 6. Integration of viral glycoproteins (gp120 and gp41) into host’s cell membrane. use of fatty acids in respiration. 8. Integration of viral glycoproteins into cell membrane 13 No integration of viral glycoproteins into host’s cell membrane. 4. A phage enzyme (lysozyme) “drills” a hole in the bacterial wall. CJC 2010 8 (a) Describe the role of glucagon in regulating blood glucose. via weak interaction between tail fibres and lipopolysaccharide (receptor site) of host bacterium. After the baseplate is firmly on the cell surface. 4.Host cell 6 Infects bacterial cells Infects human T-cells Penetration / Entry 7 Phage does not undergo fusion with host cell’s plasma membrane / contracts its tail sheath. switching off glucagon secretion 7. Uncoating of nucleocapsid to release genome and enzymes. HIV releases its nucleocapsid (ssRNA and reverse transcriptase) into cytoplasm.  1. 3. 5. (b) Describe the reproductive cycles of bacteriophages that reproduce via a lytic cycle. 2. Its ssRNA is converted to dsDNA. Attachment sites on the tail fibres of T4 phage recognize and adsorb to receptor sites on the host bacterium.
single chain made up of amino acids 1b.g ribosomes. This provides raw material for virus DNA synthesis. Phage DNA enters bacteria cytosol. 10. This marks the start of the eclipse period. Pilot protein helps phage DNA to cross inner membrane. a phage-encoded lysozyme breaks down the bacterial peptidoglycan causing osmotic lysis and release of the intact new bacteriophages leading to destruction of host cell. made up of nucleotides 2a. nucleotides held together by phosphodiester links 5a. These enzymes coded by the phage genome degrade host DNA. quoting appropriate units / location within the cell where they are synthesized or replicated / appropriate named function (b) Explain how the structure of collagen and haemoglobin are related to their function. enzymes and structural componenets using bacterium’s metabolic machinery.  Collagen 1. double helix of DNA. 12. amino acids held together by peptide linkages 4b. 15.  Structural Differences 1a. ref to details of amino acid structure 3b. 14. a linear. Replication of phage DNA occurs using the bacterium’s metabolic machinery. Synthesis of phage proteins. e. made up of monomers that consist of up to 20 amino acids 2b. Usually. Assembly of new bacteriophages around the genomes (spontaneous assembly). 16. each consisting of 3 polypeptide chains tightly twisted and wound together into a triple helix. 11. Phage genome is expressed and enzymes are produced. reference to association with histone proteins 6a. double stranded. ref. reference to collagen as a fibrous protein / quaternary structure: made up of a staggered array of tropocollagen molecules. DNA contain phosphorus 7 suitable reference to size. conformation of a folded tertiary structure 5b. may contain contain sulphur 6b. 13. [20 marks] 9 (a) Describe the main ways in which a globular protein differs from DNA. RNA and DNA). shutting down the bacterium’s gene expression and macromolecular synthesis (protein. to details of nucleotide structure 4a. only 4 bases in DNA 3a.9. Transcription of phage DNA. held by H-bonds hydrogen bonds between glycine and proline or hydroxyproline residues in different polypeptides .
alveoli in the lungs and releasing O2 in O2 -low environment e. (affinity of haemoglobin for the 4th O2 molecule is approximately 300 times that for the 1st) Generalised / motherhood statement such as protein made up of long chains of amino acids linked together by peptide bonds – to be credited only once.  With appropriate reference to integral / peripheral / transmembrane proteins. Being globular.g. 1. where they form hydrogen bonds with water 4. There is a highly irregular sequences of amino acids in the polypeptide chains. ionic bonds being involved.g. straight and unbranched (left-handed) helix that has a rigid kinked conformation. due to H-bonds between the 3 polypeptides.g. hence its important structural roles in connective tissues. Each subunit / polypeptide is attached to a Fe2+-containing haem group. reference to co-operative binding allosteric effect. the triple-stranded tropocollagen molecules run parallel one another and disulfide cross-linkages between the R-groups of the amino acid lysine holds the molecules together. haemoglobin is soluble in water to form a colloidal suspension.at high O2 tension ⇒ O2 binds as molecular oxygen to the Fe of the haem group. the tight winding of 3 polypeptides together to form a triple helix and presence of strong covalent bonds between tropocollagen molecules . which are interlocked by hydrophobic and ionic interactions 2. Each polypeptide has a regular. bones and as support in tendons. at low O2 tension. allowing the 3 helices in the tropocollgen to be tightly twisted into a triple helix 4. hence is a conjugated protein. forming long parallel fibres 5. hydrophilic amino acid residues directed outwards on the outer surface. ATPase phosphorylates ADP to ATP using energy released as H+ ions follow down a concentration gradient / cytochrome oxidase in ETC (or any appropriate example) 2. increases the affinity of the haemoglobin for oxygen and hence facilitates the binding of the 2nd O2 molelcule and so on. each polypeptide chain undergo extensive folding to form a compact.make collage a very stable structure with high tensile strength. where almost every third amino acid sequence is a glycine with high proportion of proline / hydroxyproline residues and where X may be any of various other amino acid residues 3. with examples. often follows the pattern Gly-Pro-X or Gly-X-Hyp. No credits for non-specific reference to other bonds such as hydrogen bonds. As electrons acceptors / carriers of the ETC on inner mitochondrial membrane / thylakoid membrane in chloroplast. the roles of proteins in membranes. each haem groups binds to 1 moelcule of O2 so each haemoglobin molecules can bind up to a maximum of 4 O2 molecules 5. repetitive sequence of amino acids. disulphide linkages. glycine is the smallest amino acid and this together with proline allow the polypeptide chain to be wound into a tightly coiled. where the binding of 1st O2 molecule causes a change in the conformational state of the haemoglobin molecule / a change in the position of the haem groups. reference to haemoglobin as a globular protein / quaternary structure: made up of 2 α and 2 β globin subunits. ligaments for attachment of muscle to bone Haemoglobin 1. As membrane-bound enzymes – involved in metabolic functions e. O2 is released. spherical shaped protein due to hydrophobic interactions between the (hydrophobic) R groups. all 4 polypeptide chains are linked to form a roughly globular molecule 3. using the .2. (c) Describe. to actively respiring cells 6. important in the metabolic role of Hb in red blood cells as an O2 carrier – able to bind with and pick up oxygen in O2-rich environment e. the haem group binds reversibly to oxygen to enable oxygen to be taken up and released readily . hydrophobic and hydrophilic interactions.
auaporins / as gated channel can open / close to allow cells to regulate the movement. • Codons are non-overlapping • Has spliceosome recognition sites to allow for excising of introns. Glycoproteins as surface markers for cell-to-cell recognition to identify cell type – significant in immune response/transplant / for attachment purposes: as in cell-to-cell adhesion to allow aggregation and association of ‘like’ cells into tissues.  Messenger RNA (mRNA) • Single-stranded.one for each amino acid • Has anticodons. transporting ions / molecules / solutes via passive facilitated diffusion / active transport 4. as anchors on the cytoplasmic surface for attachment to cytoskeleton AJC 2010 8 (a) Describe how the structures of RNA are adapted for translation. allowing only specific molecules to enter/exit. • Internal hydrogen bonds to form clover leaf shape/ have specific 3D configuration/ stabilize the molecule. • mRNA (5’UTR) has ribosome attachment site. bind the solute on one side of the membrane which then causing the protein to undergo a conformational change that brings the solute to the opposite side of the membrane e. As channel proteins. acetylcholine receptors associated with Na+ ion channels on postsynaptic membrane for acetylcholine for nervous transmission across synapse As transport proteins that are either specific or non-specific. UGA. As carrier proteins. to generate a proton gradient across membrane 3. UAG) codons. glucose transporter GLUT1. with specific hydrophilic domains / channels to allow passage of ions and hydrophilic / charged. • Complementary base pairing between codon and anticodons. • Has START/ INITIATOR (AUG) codon and STOP (UAA. G-protein linked receptors for glucagon / tyrosine kinase receptors on muscle cells for insulin for cell-to-cell signaling and signal transduction / ionotropic receptors that are linked to (ion) channel proteins e.g. • Has shape complementary to amino acyl tRNA synthetase for activation of amino acid. (award only once in either mRNA or tRNA discussion) (4 marks max) Transfer RNA (tRNA) • Has (3’ CCA) end to attach to amino acid/ has amino acid attachment site. • 5’ 7-methyl guanosine cap and 3’ poly-A tail to ensure mRNA stability.energy released during the electron transfer as electrons travel downhill in energy terms from one carrier to another. e. moving down a concentration gradient / as non-gated channel – providing an open passage way for movement e.g. • At least 20 different tRNAs . • One codon codes for one amino acid. (2 marks max) Ribosomal RNA (rRNA) .g. found across membranes of red blood cells for facilitated diffusion of glucose 6.g. voltage-gated Na+ channels. As surface receptors for binding of ligands / neurotransmitters / hormones e. • Mature mRNA consists of exons/ no introns.g. voltage-gate Ca2+ ion channels 5. polar molecules that cannot transverse the hydrophobic core of the phospholipids bilayer. Na+-K+ pump – a type of protein carrier that usually use ATP to move solutes against a concentration gradient (from a low solute concentration to a high solute concentration). e.g.
• Daughter DNA are genetically identical to each other. accept labelled diagram. • Complementary base pairing. • Only results in reshuffling of alleles on a chromosome. • Due to hydrogen bonding/ complementary base pairing within. • Reference to the three different bands after (CsCl) centrifuge. • Parental strands unzip/ hydrogen bonds broken. 70S.. • Involved in peptidyl transferase activity. inversion or translocation of several gene loci on a chromosome Effects on allele • Gives rise to a new allele. Ploidy • No change in ploidy • Could also result in polypoidy or aneuploidy Frequency • More frequent because genes outnumber chromosomes by several thousand to one • Less frequent Importance • Of evolutionary importance because acquisition of new alleles increase gene pool for natural selection • Of lower evolutionary importance because it only reshuffles alleles already existing in the gene pool Visibility under light microscope • Not visible • Usually visible Examples • Sickle cell anemia (due to substitution of one nucleotide) • Down’s syndrome (due to an extra chromosome 21) Any valid comparisons. duplication. (c) Explain how the Meselsohn and Stahl experiment supports the semi-conservative model of DNA replication. No of chromosome involved • Within one chromosome • Involves one or a few chromosomes Mechanisms • Brought about by deletion. • Gives rise to a variety of ribosomal types (e.g. inversion or substitution of one or more nucleotides • Brought about by deletion. (2-3 marks max) 9(a) Discuss how signal amplification is illustrated by the effect of hormone on glycogenolysis.  Reference to experimental details • DNA labeled with heavy nitrogen / 15N. 30S. then cells transferred to light nitrogen/ 14N for two generations. 50S. • Binding of one / a molecule of epinephrine / glucagon to GPCR causeds GPRC will undergo a conformation change . • Usually affect many gene products since so many gene loci involved. . (1-2 marks max) How experiment supports • Parental strands act as template. (2 marks max) (b) Distinguish between chromosomal and gene mutations.• A structural component of ribosome. missense. frameshift. insertion.  Gene Mutation Chromosomal Mutation/ Aberration Definition • Change in structure of DNA/ change in (nucleotide) base sequence/ different types of gene mutations including point. nonsense. 80S. silent • Change in structure or number of chromosomes Gene locus • Involves one gene locus • Involves a few gene loci Protein products • May or may not affect protein products (depending on whether silent mutation or in non-coding DNA regions). • New DNA molecule consists of one parental strand and one daughter strand. resulting in new protein which may have a novel function • Does not reshuffle alleles • No new allele arisen. etc).
9 (b) Describe the similarities between the interaction of a substrate with an enzyme and the interaction of a ligand with a receptor. to activation of receptor. • Both can induce a conformational change in the protein when they bind... • Ref.. 9(c) Compare between nervous and hormonal control. • Both will bind to protein via H bonds. • Binding site for receptor. • Ligand dissociates from binding site of receptor / Ligand-receptor complex are removed.. 1 mark will be deducted from the overall marks. [R: increase cAMP. each activated kinase is able to activate a large number of the next relay molecule/kinase . ionic bonds.. which is released. hence amplifying the signal. • ES complex formed will be converted to product. • the number of activated product is always greater than those in the preceding step as one move down the cascade . hence the signal is further amplified. • Each activated G-protein activate enzyme adenylyl cyclase.• to allow the activation of several / few G-protein by displacing GDP for GTP . • At each phosphorylation step/cascade. • Both are complementary in shape to sites that they bind to.. • Both interactions are not permanent. • binding of 1 glucagon to receptors will lead to the hydrolysis of large number of glycogen. each of which is able to catalyse the conversion of large number of ATP to cAMP . • Active site for enzyme.  • Both bind to specific regions of protein (idea of specific region/portion is impt). • Each activated protein kinase A will initiate a sequential phosphorylation and activation of kinases / phosphorylation cascade . hydrophobic interactions. activation of cAMP] • These cAMP in turn binds and activates large number of protein kinase A . * If less than 3 of the highlighted points are present..  Similarities: Both serve as means of communication/ allow living organisms to respond to stimulus Stimulus ◊ transmission of message ◊ effector / stimulus elicit a response Differences: Endocrine Nervous system Nature of transmission Chemical transmission (hormones) through blood system Electrical and chemical transmission (nerve impulses and chemical across synapses)mil and electrical Transmission speed Slow Slower transmission and relatively slow-acting (adrenaline an exception) Fast . to induced fit hypothesis for enzymes. • Ref. • lead to the activation of large number of glycogen phosphorylase • each will catalyse for the breakdown of large amount of glycogen into glucose.
. mRNA editing. activators to enhancer. 3. AVP. 2 polymers of deoxyribonucleotides chains twisted into a double helix.. extracellular signals like hormones. e.34nm/10 bp per complete turn.. gene silencing by miRNA. 9.g.. Chromatin remodelling 2. histones positively charged. cis-acting elements. purine-pyrimidine: 2 nm diameter. b.  Gene Amplification 1. Transcriptional control 4. . allow GTF to bind. The regulated variable is usually at a set point which can be changed by a stimulus. e. 5. 12. formed nucleosome core. ss pre-mRNA.. (b) Describe the control of gene expression in eukaryotes.. [Total: 20] 10 (a) Explain the principles of homeostasis. Homeostasis is the maintenance of a constant...Rapid transmission and response Pathway of transmission Specific (via nerve cells ) Not specific (blood around whole body) Strength of message Strength dependent on amount of hormones Impulse size same regardless of stimulus Length of response Often long-term changes (except adrenaline) Often short-term changes nothing action Target Response may be very widespread.  1. 8. with 5’ capping with modified guanine/methylated guanine.. concentration of the translated product.... 10.. 5. further coiled into a solenoid forming a 30nm fibre. e.. 2. 14..  1. Post-translational control 13.. association with proteins for nuclear export. proteins not required are tagged for ubiquination by protease. repressors to silencers á and â transcription rate. 6.. associate with H1 histone to form nucleosome. change detect by a receptor which sends signals to control center/regulator. C≡G. 2. GTFs binding to promoters and proximal promoters.. acetylation removes +ve charges from histones.. distinct polarity 3’ end with free hydroxyl group at 3C and 5’ end with phosphate group at 5C. 0. a. CpG islands. forming complementary dsRNA in DICER cplx prevent ribosomal attachment/ cleave mRNA. 4.bonds between complementary bases.. demethylation removes methyl grps from proximal promoters. duplication of genes to increase the number of copies. linked by spacer/linker DNA forming 10nm ‘beads-on-string’ structure.. held by H. the ∆ in codon results in different functional polypeptide.g. growth et organs at different parts of body Response often very localized.. 3’ polyadenylation for stability/ nuclear export of mature mRNA.g.. stability of mRNA in the cytoplasm controlled by degradation in response to presence of RNA sequence signalling degradation. binding of STF e. Translational control 11. 7. loosen –ve charged DNA. DNA molecule associated 1¾ turns with 8 histone proteins/octomer.. 9.. Post-transcriptional control 6. formed ionic bonds with negatively charged DNA. stable internal environment within an organism regardless of changes in external environment via a self-regulating mechanism. AVP. A=T. 3. futher looping in presence of scaffold proteins to form metaphase chromosomes. splicing of introns out and joining of exons forms mature mRNA by spliceosome. 7..g. 3. 3.. one muscle target organ IJC 2010 9 (a) Describe the structure of DNA and its organisation in a eukaryotic chromosome. 8.
Photosynthetic pigments such as chlorophyll a. 9. Photon of light absorbed by both PS will excite electrons in special chlorophyll a in reaction centres to higher energy levels.g. And pass on to electron carriers on the electron transport chain (ETC). Max 7 (b) Give an overview of the Krebs cycle and its significance in respiration... From the stroma into the thylakoid lumen. 6.  1. Glucagon 6.  1. 16. results in activation of glycogen phosphorylase to convert glycogen into glucose. 7. 10. Activated PKA then phosphorylates other relay proteins and enzymes. 7.. activates other enzymes in phosphorylation cascade.. protein kinase A (PKA).. 13.. (b) Describe the roles of insulin and glucagon in regulation of blood glucose. insulin released to bind to rtk receptors of effectors e. α cells in islets of Langerhans detect the drop. Depresses rate of synthesis of glucose from non-carbohydrate source via gluconeogenesis. AVP. glucagons released bind to GPCR on effector e. 8. [bld glu] â below nom. [bld glu] á above norm. of glucose transporters in the liver cells to increase uptake of glucose. 3. 15. chlorophyll b and carotenoids. 8. 5. The effect of cAMP is removed by phosphodiesterase which converts cAMP back to AMP. Accumulation of H+ generate potential energy.  Overview .g.4. 4.. through H+ channel. results in increased no.. 7. energy is released. reached set point. 5. Adenylyl cyclase catalyses the conversion of ATP to cyclic AMP (cAMP). [Total: 20] JJC 2010 8 (a) Describe the process of ATP production in the chloroplast... These excited electrons are accepted by primary electron carriers. As electrons move down the ETC. are arranged in photosystems. neg feedback mechanism prevents further release of hormones by pancreas. 4.. are embedded on the thylakoid membranes. 2. 4.. Ga simultaneously dissociates from its Gβγ. 3.. convert excess glucose to glycogen in glycogenesis by activating glycogen synthetase. H+ return to the stroma by diffusing down their concentration gradient 14. Glucagon binds to the complementary ligand-binding site on GPCR receptor causing a conformational change to receptor. Catalyzed by ATPase. β cells in islets of Langerhans detect the á. Electron carriers on the ETC are of progressively lowered energy level. GTP from the cytosol then displaces GDP from the nucleotide-binding site on Ga. 12. 6. 9. The energy released is used to pump H+. cAMP activate relay protein. 2. Energy is released and used to couple the phosphorylation of ADP + Pi to produce ATP.  Insulin 1.... 10. activates effector resulting in a response to restore set point via positive/negative feedback. Two photosystems PSI (P700) and PSII (P680) which absorbs wavelengths of 700nm and 680nm respectively. 3. liver cells. liver cells. 8. 5. 11. AVP (c) Describe the molecular events when glucagon binds to its target cell. translocate along the plasma membrane to activate the enzyme adenylyl cyclase... 2.
Per cycle.  ... involve transfer of electrons between electron carriers.. 9. Involvement of light energy Required to energize the electrons in special chl a Not required. from mitochondrial matrix to intermembrane space. Malate (4C) undergoes oxidation to form oxaloacetate (4C) 5. one molecule of acetyl CoA (2C) undergo oxidative decarboxylation. 2... 3. 6C to 5C to 4C intermediates.  Similarities: 1. Description of the decarboxylation process i. α–ketoglutarate (5C) undergoes oxidative decarboxylation to form succinate (4C)..... 8. 10. Release of hydrogens (NADH produced) which can be used in oxidative phosphorylation to provide energy to produce ATP. 2. Differences: Features Photophosphorylation Oxidative Phosphorylation Sources of energy for ATP synthesis energy for making ATP comes from light energy for making ATP comes from glucose oxidation processes. 6.. Carbohydrate intermediates can be converted to amino acids. three molecules of NADH. one molecule of FADH2 and one molecule of ATP through substrate level phosphorylation are released per cycle.. Max 3 marks (c) Compare and contrast oxidative phosphorylation and photophosphorylation. Succinate (4C) undergoes oxidation to form fumarate (4C) iv. 4.. from stroma to thylakoid space H+ pumped outwards.. α–ketoglutarate (5C) undergoes oxidative decarboxylation to form succinate (4C) iii.1. OR Citrate (6C) undergoes oxidative decarboxylation to form α–ketoglutarate (5C). energy released from electron transport is used to generate proton gradient. Location Thylakoid membrane of chloroplast Inner membrane of mitochondria.. Electron donors For non-cyclic reaction: water For cyclic reaction: PS I NADH. Citrate (6C) undergoes oxidative decarboxylation to form α–ketoglutarate (5C) ii. one molecule of oxaloacetate (4C) is regenerated to receive more acetyl groups and the cycle continues. potential energy of proton gradient is harnessed for ATP synthesis. Electron acceptors For non-cyclic reaction: NADP+ For cyclic reaction: PS I Oxygen.. Occurs in matrix of the mitochondrion.e. Max 5 marks Significance 7. Permits amino acids to enter Krebs cycle when glucose is in short supply. i.. Fumarate (4C) is converted to malate (4C) v. Completes the oxidative breakdown of glucose to CO2 and H2O and release sufficient energy... Acetyl CoA (2C) and oxaloacetate (4C) are condensed to form citrate (6C). 3. Establishment of proton gradient H+ pumped inwards.. At the end of the cycle. FADH2. Max 6 9 (a) Describe the important events that occur during Meiosis I and explain the significance of each event. Two molecules of CO2.
Telophase I & cytokinesis. 26. 16. 14.g. 4. Cause cancer due to over-expression of proteins (leading to development of malignant tumours). 11.. 20.. results in new combination of alleles . 6. Prophase I. Homologous chromosomes are pulled apart to opposite poles . genetic variation in gametes later .. and the ability to prevent absorption of therapeutic drugs. 18. Max 6 (c) Outline the end-replication problem in eukaryotic chromosomes. 8. Division of cytoplasm (and organelles) . 10. 21. 7. Allows gametes to contain a haploid set of chromosomes . 27. 4. furrowing (animal cells) / cell-plate formation (plant cells) . 5. 24. following fertilization . E.Important events during Meiosis I Significance 1. DNA polymerase. can only add nucleotides to the 3′ end. 19. 2. 13. These amplified genes can be transcribed and translated OR leads to an overproduction of the corresponding mRNAs and proteins. 5. If an oncogene is amplified.. 23. Gene amplification refers to the process of (selectively) increasing the number of copies of a particular gene (located at a particular region of the chromosome).  1. pairing of homologous chromosomes.  1. (b) Describe the significance of gene amplification. thus drug-resistant tumors can continue to grow and spread even in the presence of chemotherapy drugs. In the developing ova of eukaryotes. 9. Anaphase I. 22. 3. Allows formation of 2 haploid daughter cells . Allows gametes to contain a random combination of paternal and maternal chromosomes . 8. 2. 17. Synapsis . without a proportional increase in other genes. for restoration of diploid no. to form tetrads / bivalents .. of chromosomes . conferring them with drug resistance. of a elongating/pre-existing polynucleotide/primer. Meet the needs of cells resulting in higher level of mRNA and polypeptide synthesis at different development stages of cells. Preparation of cells for Meiosis II . Allows for exchange of genetic material . Crossing over .. alignment of each homologous pair is independent of other homologous pairs / independent assortment . 28. Homologous chromosomes are arranged along equator in pairs . 25.. movement of each homologous pair is independent of other homologous pairs / random segregation . Allows gametes to contain a random combination of paternal and maternal chromosomes . genetic variation in gametes later . Genes related to drug resistance in these cancer cells are increased. between non-sister chromatids of homologous chromosomes . formation of chiasmata . 15. 3. 7. 3. . This allows the ova to make enormous numbers of ribosomes resulting in a burst of protein synthesis once the ova are fertilized. million or more additional copies of rRNA genes are synthesized. 2. Confer selective advantage which allow organisms to survive in a particular environment.. An example is the amplification of the ErbB-2 oncogene in breast and ovarian cancers. 12. Allows for alignment of genes on chromosomes . genetic variation in the gametes later . Metaphase I. to prepare for crossing over between the homologous regions later . 6. 9. 10. then the resulting over-expression of that gene can lead to de-regulated cell growth.
Eukaryotic chromosomes are made highly compact with the involvement of many histones while comparatively. Prokaryotic chromosomes are usually singular and carry the entire genome while usually several eukaryotic chromosomes make up the entire genome. the position of the regulatory and structural genes. with each chromosome carrying a small proportion of the eukaryotic genome. . Transcription (and translation) continues until all/most of the lactose are digested to produce glucose and galactose. 5. The repressor has two binding sites – DNA binding site and repressor binding site (referred to as allosteric site). LacZ is transcribed and translated to produce β-galactosidase. and repressor binds to the operator site again. Accurate reference to glucose and CAP-binding site: 1 mark max. where several genes are under the control of a single promoter. Causes a conformational change in the repressor. Eukaryotic chromosomes contain a high proportion of non-coding DNA such as introns. They consist essentially of the same types of nucleotides – adenine. Operator site overlaps with promoter site. and LacA produces transacetylase. primer at 5’ end. Both are compacted and associated with proteins that help to pack them. and other intergenic regions such as satellite DNA. Allolactose binds to the Lac repressor bound to the operator of the Lac operon. telomeres. removed. because no 3’-OH available (to which a DNA nucleotide can be added). The structural genes of prokaryotic chromosomes are organised in operons. which are almost absent in prokaryotic chromosomes. Trace amounts of β-galactosidase (minimally transcribed / expressed) converts lactose to allolactose as a side reaction. prokaryotic chromosomes are loosely packed with the involvement of some histone-like proteins. Eukaryotic chromosomes have multiple origins of replication while prokaryotic chromosomes have only one.inducible) Trace amounts of lactose permease (minimally transcribed / expressed) on cell surface membrane of prokaryote permits the entry of lactose. (b) Compare and contrast the structure and organisation of prokaryotic and eukaryotic chromosomes. glycosidic. whereby the operon is regulated via a repressor (negative). as well as promoter and operator). 8. YJC 2010 8 (a) Describe how the presence of lactose results in the transcription of the Lac operon in prokaryotes.  Correct diagram of the Lac operon (in particular. and presence of lactose induces the transcription of the operon (normally not transcribed . 5’ end of the DNA becomes shorter relative to that of the previous generation. The Lac repressor is a protein that is transcribed and translated from LacI gene (regulatory gene) located in front of the promoter site. cytosine and guanine. centromeres. LacY produces lactose permease. Differences (max 5) Prokaryotic chromosomes are circular while eukaryotic chromosomes are linear. They are composed of DNA double helix structure.  Similarities (max 3) They both have origins of replication that allow for them to be replicated. 6. thymine. but cannot be replaced with DNA/ gap cannot be filled in. while the structural genes of eukaryotic chromosomes are each under the control of a single promoter. preventing it from being attached to the operator site (releasing it from the DNA binding site). Description of negative inducible mechanism. 7.4. hydrogen. Similar kinds of bonds can be found in the chromosomes – phosphodiester. RNA polymerase binds to the promoter site and transcribes the structural genes.
of named tumour suppressor gene: P53. covalent disulphide bonds. Types of mutations causing loss of function Gene mutation (any named kind). Initiate apoptosis (programmed cell death).C). 10 Levels of organization 4 levels 1 structure/a-helix. 7 Bonding (2) Polypeptide chains/subunits linked by ionic bonds.T. 5 Bonding (1) Linked by peptide bonds Linked by phosphodiester bonds.Eukaryotic chromosomes are bounded by nuclear envelope whilst prokaryotic chromosomes are not enclosed by the envelope (found in the nucleoid region) and are usually attached / anchored to cell wall. 3 Monomers Amino acids deoxyribonucleotides. Description of cell activity resulting from loss of function DNA damage not repaired for proteins regulating cell cycle leads to cell division. Mutation in regulatory sequence.  9 (a) Explain the main ways in which a globular protein differs from a sequence of DNA.G. 6 Number of subunits One or more Always 2 under physiological conditions. Normal functions of tumour suppressor gene: Activate DNA repair. 13 Process of synthesis transcription and translation DNA replication 14 Template for synthesis mRNA DNA /parent DNA . 4 Types of monomers 20 used in humans 4 types (A. 2 Solubility in water Yes No/less soluble.g.  E. structural. 12 Location Everywhere/both inside and outside the cell Only inside the cell /in nucleus. Both copies of alleles to be mutated in order for the cancer phenotype to be expressed (loss of function). Cancer cells do not undergo apoptosis and carries on dividing. hydrophobic interactions and hydrogen bonding Only hydrogen bonding links the two DNA chains. 8 Function Multiple functions: Enzymatic. negative or neutral) Negatively charged. 9 What confers functionality Its function is usually linked to its 3D shape/conformation and configuration Its function is dependent only on the order in which the monomers are arranged in DNA chain. energy source (any 2) Carry hereditary information/code for synthesizing products. transport. Inducing mitotic arrest (stopping of cell cycle). 11 Charge Can be of any charge (positive. (c) Explain how mutations related to a named tumour suppressor gene lead to cancer. Checkpoints of mitosis not regulated resulting in continuous cell division.  Pt of comparison Globular proteins DNA 1 Shape Compact & round Reject Globular Linear in eukaryotic cells Note that prokaryotic cells have circular DNA.
Glucose units are linked in a linear way with α(1→4) glycosidic bonds. Highly branched structure (more so than starch) increases its solubility in water and allows for the rapid synthesis and degradation of glycogen. Packing and relation to function Coil helically with multiple branching into a compact structure thus can be stored in large amounts within a fixed volume. The bonds cannot be broken down by hydrolysis easily. Branching takes place with α(1→6) glycosidic bonds occurring every 24 to 30 glucose units The bonds can be broken down by hydrolysis easily. Association with water and relation to function The hydroxyl groups (-OH) on the glucose residues on amylopectin are used to form hydrogen bonds with adjacent chains. thus providing tensile strength for cell wall. Branching takes place with α(1→6) glycosidic bonds occurring every 24 to 30 glucose units. . Glucose units are linked in a linear way with α(1→4) glycosidic bonds. Due to position of the hydroxyl groups (-OH) on the glucose residues. Amylose forms a colloidal dispersion in hot water (which helps to thicken gravies) whereas amylopectin is completely insoluble. it is a highly branched polymer of glucose.(b) Outline the main differences in structure and function between starch.suitable as structural carbohydrates.  Similarities All three are polymers made up of glucose molecules Differences Starch glycogen Cellulose Types of bonds and significance to function Amylose is a planar polymer of glucose linked mainly by α(1→4) glycosidic bonds Amylopectin is a highly branched polymer of glucose. Form fibrils / fibers. The bonds can be broken down by hydrolysis easily. thus does not affect the water potential of cells. cellulose and glycogen. Insoluble in water. each successive glucose residue in the chain is rotated at 180° to allow the formation of β(1→4) .suitable as a energy store Cellulose is a polysaccharide consisting of a linear chain of several hundred to over ten thousand β(1→4) glycosidic links.suitable as a energy store glycogen is highly similair to amylopectin.
2. Basic level ◊ “Beads-on-a-string” model where DNA wind around histone proteins to form nucleosomes.  (c) Describe various ways in which gene expression may be controlled at translational and post-translational level. There are two main ways: 1. Differences between prokaryotic and eukaryotic genome Prokaryote Eukaryote Genome description Circular/closed loop linear chromosome. Packing of DNA (2 marks) Packing also take place but not as extensive. Both shows different levels of packing to compact the genome such that they can fit into the cell. (Contains a few million bp. found in nucleoid region. . Both consist of double stranded DNA. (Contains tens of millions to hundreds of millions of base pairs (bp) in length. (This arise the need for post-transcriptional modification ◊ RNA splicing.  Compare the structure and organization between prokaryotic and eukaryotic genome. DNA-binding proteins are involved in holding the loops in place. They can be translated immediately.  (c) Describe the experimental evidence for semi-conservative replication.) No of ori 1 origin of replication on 1 chromosome. (mRNA formed during transcription need not be processed.) Typically longer chromosome.Large intermolecular spaces. Each chromosome consists of several origin of replication. Repetitive sequences are commonly found near. AND 2.  9 (a) Describe the structure of DNA and tRNA. Multi-levels of packing. Supercoiling of the looped DNA. centromeric and telomeric regions but may also be throughout the chromosome Genes organization Coordinately controlled genes are often clustered into an operon.  (b) Describe the eukaryotic processing of pre-mRNA.) Introns (non-coding. (in contact with cytoplasm). thus allow water to move through the cell wall PJC 2010 8 (a) Compare the structure and organization between prokaryotic and eukaryotic genome. Formation of looped domain – a segment of DNA that is folded into a loop-like structure.) Chromosome location Chromosome not in nucleus. (A transcriptional unit consisting of . Size Shorter. Nucleosomes undergo further packing to form 30 nm fibre/solenoid ◊ 300 nm fibre Introns Introns not found within genes. repetitive sequences) found interspersed within a gene. The chromosomal DNA must be compacted about 1000-fold in order to fit into the bacterial cell. Similarities: 1.  (b) Describe the process of DNA replication in prokaryotes. Chromosome found in nucleus. Location of repetitive sequences Repetitive sequences interspersed throughout the chromosome.
recognize these splice sites. 13. 2. poly (A) polymerase (PAP). Several different snRNPs join with additional proteins to form an even larger assembly called a spliceosome.adding of sugar/lipids/phosphate group. 9. 14. The 5’ end. Chemical modification 8.coordinately regulated clusters of genes with related functions. Enzymes in the proteasome cut the proteins into small peptides◊ degrade by other enzymes in cytosol. . 16. Global control translation initiation 3. 9. 8. mRNA degradation 5. Particles called small nuclear ribonucleoproteins or snRNPs. 16. Chemical modification. 4. A polypeptide will coil/fold forming function 3D prot with secondary & tertiary structure (cisternae of RER).) Coordinately controlled genes are organized not in clusters but interspersed throughout the genome.. ubiquitin protein is tagged. At the 3’ end. snRNPs are located in the cell nucleus and are composed of RNA and protein molecules. an enzyme. Block translation initiation. 5. Allows nuclease enzymes to rapidly digest the mRNA. Post. Leads to recognition by large proteasomes. The spliceosome interacts with the splice sites at the ends of an intron. 3. snRNA plays a role in the catalytic process as well as in spliceosome assembly and splice site recognition. Protein processing control the type of proteins to be formed. intron region was looped out 14. 15. 11. is immediately capped off with a modified form of a guanine nucleotide. Control the lifespan of mRNA in the cytoplasm ◊ the amount of proteins formed. 7. is bound to the RNA polymerase II before transcription starts. Cell surface proteins must be transported to target destination to function. Protein degradation 12. each molecule is about 150 nucleotides long. Absence of plasmid Differences 7 max 1. To mark a protein for destruction. The signals for RNA splicing are short nucleotide sequences at the ends of introns. 6. 13. 11. makes a poly(A) tail consisting of 50 to 250 adenine nucleotides. It cuts at specific points to release the intron. 4. Activation /inactivation of one or more of TIF(translation initiation factors) (by phosphorylation/dephosph). Prevent attachment of small ribosomal subunit to mRNA. The RNA in a snRNP particle is called a small nuclear RNA (snRNA). 12.transcription modification is required to process the pre-mRNA to form mature mRNA and to facilitate the export from nucleus to cytoplasm. Translation will be initiated for ALL the mRNA in a cell. where there is polyadenylation sequence present 6. each with own promoter. Enzymes (3’◊5’ exonucleases) breaks down poly (A) tail first. 18. Followed by enzyme removal of 5’ end (decapping) ◊ critical step. 2. then immediately joins together two exons that flanked the intron. 10. Regulatory proteins binds to specific sequence within the 5’ UTR. Protein degradation affects the amount of protein present in cell. Promote/ Inhibit the formation of translation initiation complex. 10. 17. 19. max 6 (c) Gene expression may be controlled at translational level via these processes: Process involved Mechanism Regulation Gene expression control of during translation initiation 1. Gene expression may be controlled at post translational level via these processes: Process involved Mechanism Regulation Post translational modification Protein processing (during translation). the end made first during transcription. 7. The enzymes required for capping is grouped to form the Capping Enzyme Complex (CEC) and. 15. Cleavage of initial pro-insulin (polypeptide) into active hormones. plasmid An extrachromosomal plasmid is usually found in prokaryotes.
8. Removal of RNA primer leaves substantial gaps between the DNA fragments. 9. with the nitrogenous bases arranged as side groups off the chains (project into the centre of the double helix). 6. 2. ie. The unwinding DNA chains provide templates for the synthesis of new DNA chains. 3’ end of the tRNA always ends in the base sequence of CCA 4. 5’ end of the tRNA always ends in a base. Such primers are necessary because the enzyme. 7. After parental strand separation. 3. Hydrogen bonding can occur only between a purine and a pyrimidine. 4. (about ten ribonucleotides long). Formation of RNA primer 9. held together by phosphodiester bonds. Acts as an intermediate molecule between the triplet code of mRNA and amino acid sequence of polypeptide chain. 8. Topoisomerase helps to prevent over-straining of the replication fork. guanine. DNA polymerase III recognises the bases and selects free deoxyribonucleotides that are complementary to those on the . One complete turn of the double helix is 3. The two chains are said to be complementary. single-stranded binding protein (SSB) binds to the unpaired DNA strands. between the sugar of one nucleotide and the phosphate group of the next nucleotide. allowing replication to take place at both ends. stabilizing them. that is responsible for the synthesis of DNA. 5. The new DNA strand will start from the 3’end of the RNA primer. the width of a purine plus a pyrimidine. Carries the correct amino acid to the forming polypeptide chain on the ribosome. Single stranded RNA 2. Thus the sequence of bases in one chain determines that in the other chain. Once synthesis of the new DNA chain starts. 11.4 nm and comprises 10 base pairs tRNA Structure 1. they can only add nucleotides to the end of an already existing chain that is base-paired with the template strand. The enzyme primase catalyses the synthesis of a short RNA primer.34nm 11. Mechanism is by semi-conservative replication. the RNA primer is hydrolysed (removed) by enzyme DNA polymerase I (DNA pol I). The two chains run in opposite directions (antiparallel) and 6. 6.Structure: 1. known as a replication fork (bidirectional) 7. 10. One loop contains a triplet of bases called an anticodon which pairs with the complementary codon on mRNA. 12. causing the two DNA chains to separate. The separating DNA results in a “replication bubble”. 4. DNA polymerase III (DNA pol III). Wound into clover-leaf shape with 3 loops 3. 7. are held together by hydrogen bonds between their nitrogenous bases. The two chains coil round each other to form a double helix. Each chain consists of a sugar-phosphate backbone. 9. 5. The filling of these gaps by deoxyribonucleotides is also catalysed by DNA pol I Synthesis of new DNA strand 13. Along the axis of the molecule the distance between adjacent nucleotides is 0. 10. and binds an amino acid 5. The DNA molecule consists of two deoxyribonucleotide chains 2. Replication of DNA begins at specific sites called the origins of replication (Ori). The enzyme helicase causes the DNA molecule to unwind and unzip/the hydrogen bonds between the bases to break. The width between the two chains is constant (2nm) and is equal to the width of one base pair. There are more than 20 different tRNA molecules in a given cell. 8. cannot initiate synthesis of a polynucleotide. each carrying a specific amino acid. (b)Unwinding DNA double helix 1. Activated deoxyribonucleotides and transported into the nucleus via pores in the nuclear envelope 3.
DNA. Meiosis produces genetically varied gametes 2. was then centrifuged 9. C and D. 5. called the leading strand. 18. allowed to divide once and therefore the DNA replicates once. Centromeres divide resulting in separation of sister chromatids 6. Tube A contains only heavy DNA because the bacteria are grown for many generations in a medium (A) containing 15N. all the DNA molecules became labeled with 15N.  1. The cells were then transferred to another medium containing normal nitrogen (14N) and 6. Leading to formation of genetically varied organisms due to random fusion of gametes 3. and the other at the intermediate density position. Two genetically identical cells are produced when the cell membrane furrows in. (c) 1. 15. At the end of the replication. Kinetochore microtubules attach to kinetochores on the centromere 4. Prophase 1: crossing over between homologous chromosomes result in new combination of alleles 4. Cells were then allowed to divide a second and third time.template strand. 1 band on top at the same density position as the light DNA. cytosine pairs with guanine and vice versa. Tube C contains both light and hybrid DNA in the ratio 1:1 and 15. DNA pol III must work along the other template strand in the direction away from the replication fork. Tube B contains only hybrid DNA with one band occupying the intermediate density position 14. 14. 21. both the parental and daughter strands rewind into a double helix. Sister chromatids. Exact alignment of sister chromatids on metaphase / equatorial plate 5. now as chromosomes. in tube D the ratio is 3:1. Both daughter strands are synthesized in the 5' to 3' direction. (points 12 to 15 – need to explain or annotated diagram) TPJC 2010 QUESTION 8 (a) Explain how mitosis produces genetically identical cells. To elongate the other strand in a 5’ to 3’ direction. The width of the DNA bands and their positions in the centrifuge tubes reflect the amount of the various types of DNA molecules (or diagram) 12. When cultures of bacteria are grown for many generations in a medium containing heavy isotope of nitrogen (15N). DNA in the centrifuge tubes appeared as narrow bands when examined under ultraviolet light 11. 8. 16. DNA ligase catalyses the formation of phosphodiester bonds between two Okazaki fragments. which is used to make the nitrogenous bases so all the DNA became labeled with 15N 13. Messelson and Stahl experiment 4. One of the daughter strands. Max 6 (b) Describe the role of meiosis in natural selection. with CsCl2 10. The new DNA molecule consist of 1 parental and 1 newly synthesized daughter strand. move to opposite poles of the cell 7. is synthesized continuously/ towards replication fork 17. 3. 7. Similarly. The enzyme. 8. Both tubes have 2 bands. Semi-conservation replication ◊ both DNA strands are template for DNA synthesis of new strands and 2. The DNA strand is called the lagging strand. Replication of DNA during S-phase of interphase 2. Definition of genetically identical cells – some number and type of chromosomes. 20.  1. To produce genetically identical sister chromatids attached via centromeres 3. The new DNA molecule consist of 1 parental and 1 newly synthesized daughter strand. extracted from cells of A. synthesised in the form of short fragments called Okazaki fragments 19. Adenine pairs with thymine and vice versa. B. Metaphase 1/anaphase 1: independent assortment of chromosomes occur to result in gametes randomly distributed to either .
a condition called aneuploidy. 2. a condition called euploidy (polypoidy). Anaphase 1: segregation of homologous chromosomes to both poles will result in the formation of haploid gametes 6. This is known as non-disjunction. Results in the synthesis of mutated gene products which leads to uncontrolled cell division leading to cancer/increases chances of cancerous growth [R: uncontrolled cell division. 3. point mutation (e. the environment will select the organisms which has selective advantage 8. sterile. Award marks for example given: variation amidst finches allow speciation etc (c) Explain how one named factor increases the chances of cancerous growth. reproduce and pass on their alleles to their offspring 9. there must be a varied gene pool 7. little facial hair. Klinefelter’s syndrome (XXY) ¬ Failure of X chromosome to separate during oogenesis in female. Chromosome mutation: Changes in chromosome number • These changes may involve the loss or gain of single chromosomes. Aneuploidy • Loss of gain or single chromosomes eg. ¬ Symptoms – male with female characteristic. 3. breasts may develop. In the presence of an environmental change. Evolution will not occur OR promotes speciation 11. Turner’s syndrome (XO) ¬ Sterile female. Damage to DNA which cannot be repaired 4. Lack of genetic variation may lead to death of all members in the population due to the selection pressure present OR variation allows continuation of the species in the presence of chances in the environment / increase frequency of alleles in the population 10. Any named example: 1. (2n+l). or pairs of homologous chromosomes to separate during anaphase I of meiosis. • Or the increase in entire haploid sets of chromosomes. Down’s syndrome (Mongolism) ¬ Presence of an extra chromosome no.  1. For natural selection to occur. characteristic folds of skin over the inner corner of the eye. short stocky body. • Produces a change in the genotype and may result in the change in appearance of a characteristic in a population. Mutation to proto-oncogenes / tumour suppressor genes 5. arrangement or structure of the DNA of an organism. ¬ Related to the age of the mother’s egg cells. Definition of Chromosomal mutations • Result of changes in the number and structure of chromosomes.). (n-1).poles of the cells 5. low intelligence. thick neck. .g.g. Gives any form of example of how DNA can be mutated e. Named factor: ionizing radiation / UV light / tar in cigarette smoke etc 2. ¬ Symptoms – mental retardation.] Question 9 (a) Explain briefly what is meant by the terms gene mutation and chromosome mutation. (2n-1) • Result from the failure of a pair. This organisms will be able to survive. 21 in the cells. (n+l). testes very small. translocation of DNA to active promoters etc. Definition of mutation: • Change in the amount.
• Caused increased cell proliferation. • In addition.¬ Lacking normal secondary sexual characteristics. 4. ¬ If chromosomes are doubled. loss of balance. Acute myelogenous leukaemia (AML) • Chromosomal inversion on chromosome 16 • Results in cancer 4. Allopolyploids ¬ An individual with increased chromosome number derived from different haploid sets. poor motor skills and muscle atrophy. ¬ Can be induced by using colchicine.diploid hybrid ( sterile ). ¬ Autopolyploids can be fertile if they have an even number of chromosome sets. Deletion: removes a chromosomal segment 2. . Chronic myelogenous leukaem ia (CML): • Translocation • Most of the chromosome 22 has been transolcated onto the long arm of chromosome 9.. non-homologous one 4. polyploids 2n. 3n. Autopolyploids ¬ An individual with more than 2 sets of chromosomes all derived from the same species. b. Translocation: moves a segment from one chromosome to another. XYY ¬ Male. • More common in plants than animals • Associated with hybrid vigour • 2 forms: a.. allopolyploid. Duplication: repeats a segment Any named example: 1. Cri-du-chat syndrome: • deletion in the short arm of chromosome 5 • child is physically and mentally retarded 2.. reduced apoptosis ◊ cancer 3. chromosomal duplication on chromosome 17 • High gene dosage of myelin sheath protein resulting in abnormal structure and function of the myelin sheath • Symptoms: weakness of lower foot. Charcot-Marie-Tooth syndrome (CMT) • In one form. the small distal portion of chromosome 9 is translocated to chromosome 22.. each member has another to pair up with and meiosis proceeds normally -. Chromosome mutation: Changes in structure 1. XXX ¬ Female. normal appearance ¬ Fertile but mentally retarded 5. Inversion: reverses a segment within a chromosome 3.fertile. may possess psychopathic traits or tendency for petty criminal acts Euploidy (Polyploidy) • Cells contain multiples of the haploid number of chromosomes ie. variable intelligence. ¬ Many inter-species hybrids are sterile because chromosomes do not pair up at meiosis .
mRNA 5’ AUG AAG UUU GGC UAA 3’ Protein met– Lys– Phe – Gly (i) Frameshift mutation causing immediate nonsense mRNA 5’ AUG UAA GUU UGG CUA A 3’ . Sickle Cell Anaemia (iii) Non-sense Mutations • Cause a change in codon for amino acid to stop codon • Result in premature termination of translation. E.g.g. DNA: 3’-CCG-5’ ( 3’-CCA-5’ mRNA: 5’-GGC-3’ ( 5’-GGU-3’ • Glycine is still produced • OR if new amino acid have properties similar to that of replaced amino acid (ii) Missense Mutations • If mutation occurs in crucial areas. insertion. non-functional protein is formed (b) Inversion (C) Frameshift Mutation • Due to the insertion/ deletion of nucleotide pairs • Have a more disastrous effect as it cause ribosome to read incorrect triplets from point of mutation • Result in shorter chain ad/ or mostly non-functional proteins E. deletion.Gene Mutation Definition of Gene mutation • Sudden and spontaneous changes • Change in the nucleotide sequence of DNA: Duplication. inversion or substitution of bases Effects: • Alteration in a sequence of nucleotides ◊ Change in amino acid sequence of polypeptide chain ◊ affect phenotype of individual ( may be inheritable Types: (a) Substitution -1 nucleotide is replaced by another Effects: (i) Silent Mutation • Due to degeneracy of genetic code • E. E. active site of enzymes • Result in useless/ less active protein that impairs cellular function.g.g.
• correct ref.g. allopatric.C. • geographical isolation. to gene pool. • through transformation. to definition of species. • change to allele frequencies. sympatric.  • largely because bacteria reproduce very quickly. to populations prevented from interbreeding. day active/ night active.  (c) Outline the role of isolating mechanisms in the evolution of new species.g. • through transduction. whereby transfer of antibiotic resistance genes occurs across a mating bridge. 2α and 2β globin chains • Chains are encoded by 2 different genes on 2 different chromosomes Normal S. • through conjugation. islands/ lakes/ mountain chains / idea of barrier.-ValSolubility Soluble Less soluble At low [O2] Remain soluble Crystallize into rod-like fibres Shape of RBC Round. • over time sufficient differences to prevent interbreeding. • ref.3 nucleotides: no Frameshift BUT additional/ missing amino acid mRNA 5’ AUG UUU GGC UAA 3’ Protein met– Phe – Gly Case Study: Sickle Cell Anaemia Normal Adult: Haemoglobin (Hb A) • Quaternary protein with tetramer consisting of 2 different types of polypeptide chain. • ref. • ref. • ref.Protein met– STOP (ii) Frameshift mutation causing extensive nonsense mRNA 5’ AUG AAG UU|G GCU AA 3’ Protein met– Lys– Leu. whereby (defective) bacteriophages transfer bacterial genes / antibiotic resistance genes.Ala(iii) +/ . Max. • e.  • ref. whereby antibiotic resistance genes taken up by competent bacterial cells through transient pores in the bacterial cell wall. biconcave Sickle shape (b) Explain how mutations for antibiotic resistance spread so rapidly among bacteria. to examples e. • isolated populations subjected to differential selection pressure/ conditions. • mutation can be quickly passed on to large numbers of descendents (usually) via plasmids during binary fission. behavioural barriers (within a population).A Gene 3’-CTT-5’ 3’-CAT-5’ Codon on mRNA 5’-GAA-3’ 5’-GUA-3’ Polypeptide -Glu. • ref. [ 6 max ] 2010 YJC . to example organism. • ref. • ref. to reproductive isolation.
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