1) INITIATION Bozeman Science,2018

 In the nucleus, RNA polymerase

binds at promoter on DNA. It
unwinds and unzips the the double
helix of DNA .
 It moves along te direction of
transcription on DNA.
 RNA polymerase breaks the
hydrogen bond between
complementary nitrogenous bases.
 Both DNA strands separated into
single strand and one of the DNA
strand is used as a template.

2) ELONGATION
 RNA polymerase add nucleotide in
the direction 0f 5’ to 3’ end and a free
ribonucleotide (complementary to
the base) on the template strand.
 Uracil pair wih Adenine ( DNA ),
Cytosine pair with Guanine.
 DNA-RNA hybrid is temporarily
Template strand formed.
 Newly synthesized mRNA (upstream)
detaches from DNA template

3) TERMINATION
 Elongation will continue until the RNA
polymerase encounters a stop
(termination) sequence in the gene.
 When the RNA Polymerase reaches the
terminator it signals the RNA
Polymerase to stop and release from
the DNA.
 Once separated the two DNA strands
Released
come back together and reform the
pre-mRNA
double helix
 The newly formed pre-mRNA molecule
is then released

__ : location REFERENCE

__ : products  Eric j. simon, jean l, dickey, Clemson university jane .b, reece, Berkeley. (2019).

__ : enzyme involved Campbell essential biology (7 edition). California. Pearson

__ : template  https://courses.lumenlearning.com/bio1/chapter/reading-steps-of- genetic-

Transcription
__ : types of RNA involved
 EXAMPLE OF PROTEIN

Protein: Insulin

3) TERMINATION Function: helps control blood glucose

 Elongation continued until a stop codon (UAA, UAG,, levels
UGA) is reached the A site Level: quarternary structure
 A stop codon in the mRNA is recognized by a protein
release factor. Classification: globular protein
 A ribosomal enzyme then breaks the bond between Site of protein synthesized: only in Beta
the polypeptide and the tRNA in the P site, releasing cells in the pancreas
the polypeptide( protein)
 Other ribosomal enzymes separate the ribosomal
subunits and free the intact strand of mRNA.

3
LadyofHats , 2008

Large
ribosomal
subunit

Small ribosomal
subunit
1) INITIATION
 In cytoplasm,small ribosomal subunit and the
initiator aminoacyl-tRNA binds to mRNA at start
codon
sm(AUG) to form an initiation complex
 This tRNA, carries the amino acid methionine
which is the first amino acid in a polypeptide.
Aminoacyl-tRNA-synthetase attaches amino acid
to tRNA.
Bozeman
 The large Science.2018
ribosomal subunit joins the initiation
complex, with tRNA now accupying the P site
(peptidyl site).
 Initiation factor (protein) are needed to assemble
the components together and the energy is
provided by hydrolysis of GTP
2) ELONGATION
 The aminoacyl-tRNA with specific amino acid binds to
the codon in empty A site (aminoacyl site) of ribosome.
 When a complementary tRNA binds to the A site,
ribosomal enzymes remove the amino acid from the
tRNA at the P site and attach it to the amino acid
delivered to the A site by forming a peptide bond.
catalysed by peptidyl transferase.
 The ribosome then moves one codon farther along the
mRNA strand. The tRNA that was in the P site
(anticodon UAC) now enters the E site. It also exposes a
new codon in the A site. The released tRNA can now
bind another amino acid of the same type and repeat
the cycle.