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Biological Science Canadian 2nd

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Freeman, Biological Science, 2Ce, Chapter 7 Instructor Guide − 1

Chapter 7 – Inside the Cell

Learning Objectives: Students should be able to …


• Describe the structure and function of individual cell components.
• Explain what molecular “postal codes” are and how they function.
• Describe the structural and functional importance of the cytoskeleton.
• Explain the dynamic nature of the cell.

Lecture Outline
I. Bacterial and Archaeal Cell Structures and Their Functions
A. A revolutionary new view (Fig. 7.1)
1. Bacterial cells are highly organized, with an array of distinctive
structures.
B. Prokaryotic cell structures: a parts list
1. The bacterial chromosome is found in a localized area of the cell
called the nucleoid.
a. The single circular chromosome consists of a DNA molecule
associated with a few proteins.
b. In order to fit within the nucleoid, the chromosome is
supercoiled. (Fig. 7.2)
c. Some bacterial cells have additional circular, supercoiled DNA
molecules called plasmids that carry genes that help cells adapt
to unusual circumstances.
2. Bacterial ribosomes are the sites of protein synthesis.
3. Many bacterial species have internal photosynthetic membranes
that convert solar energy into chemical energy. (Fig. 7.3)
4. Bacterial organelles perform an array of tasks.
5. Canadian Research 7.1: Bacterial cells have their own
cytoskeleton. (Fig. 7.4)
6. The plasma membrane separates life from nonlife.
7. Some bacteria have flagella that are used to power movement.
8. The cell wall protects the bacteria from osmotic stress. (Figs. 7.5
and 7.6)
II. Eukaryotic Cell Structures and Their Functions
A. The benefits of organelles
1. Eukaryotic cells are compartmentalized by membrane-bound
organelles.
a. Compartmentalization separates incompatible chemical
reactions.
b. Compartmentalization increases efficiency inside the cell in two
ways:
(1) It allows for the maintenance of high concentrations of
reactants.

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Freeman, Biological Science, 2Ce, Chapter 7 Instructor Guide − 2

(2) It clusters enzymes and reactants together, thus shortening


the diffusion distance.
2. Prokaryotic versus eukaryotic cells (Summary Table 7.1)
a. Eukaryotic chromosomes are inside a membrane-bound
nucleus.
b. Eukaryotic cells are usually much larger than prokaryotic cells.
c. Eukaryotic cells have extensive amounts of internal membrane.
d. Eukaryotic cells feature a diverse and dynamic cytoskeleton.
B. Eukaryotic cell structures: a parts list (Fig. 7.7)
1. Nucleus (Fig. 7.8)
a. The nucleus is the largest organelle in the cell.
b. It is enclosed by a double membrane called the nuclear
envelope.
c. It has a nuclear envelope that is supported by the nuclear
lamina.
d. It contains the genetic information of the cell, DNA.
e. It contains the nucleolus, the site of rRNA synthesis and
ribosome assembly.
f. The nuclear envelope is continuous with the endoplasmic
reticulum.
2. Rough endoplasmic reticulum (Fig. 7.9)
a. The rough endoplasmic reticulum (RER) is a network of
membrane-bound sacs and tubules.
b. The RER has ribosomes bound to the cytoplasmic surface on
which secreted and transmembrane proteins are made.
c. In the lumen of the RER, newly manufactured proteins undergo
folding and other types of modification.
3. Smooth endoplasmic reticulum (Fig. 7.10)
a. The smooth endoplasmic reticulum is a portion of the ER that
does not have ribosomes attached.
b. It contains enzymes that are involved in the synthesis of lipids,
detoxification of harmful substances, andstorage of calcium
ions.
c. The ER (smooth and rough), the Golgi apparatus, and
lysosomes make up the endomembrane system, which is the
primary centre for protein and lipid synthesis.
4. Golgi apparatus (Fig. 7.11)
a. The Golgi apparatus consists of flattened membrane sacs
called cisternae.
b. It has polarity: a cis side that receives proteins from the rough
ER and a trans side oriented toward the plasma membrane that
ships proteins to their final destination.
5. Ribosomes (Fig. 7.12)
a. Ribosomes are found attached to the RER and scattered
throughout the cytosol.

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Freeman, Biological Science, 2Ce, Chapter 7 Instructor Guide − 3

b. They are complex molecular machines that manufacture


proteins.
c. Because they are not membrane-bound, ribosomes are not
considered organelles.
6. Peroxisomes (Fig. 7.13)
a. Peroxisomes are centres for oxidation reactions.
b. They generate hydrogen peroxide as a by-product of these
reactions.
c. They contain an enzyme, catalase, which converts hydrogen
peroxide into water and oxygen.
d. Plants have special peroxisomes called glyoxosomes that
convert the products of photosynthesis into storable sugars.
7. Lysosomes (Fig. 7.14)
a. Lysosomes function as digestive centres in animal cells.
b. Lysosomes have a proton pump in their membrane that keeps
the lumen acidic.
c. They contain digestive enzymes, called acid hydrolases, which
work best in acidic conditions to hydrolyze macromolecules.
d. Lysosomes receive material destined for hydrolysis via three
mechanisms: (Fig. 7.15)
(1) Phagocytosis: the plasma membrane of a cell engulfs a
smaller cell or food particle, forming a structure called a
phagosome that is delivered to a lysosome for digestion
(2) Autophagy: the delivery of damaged organelles to
lysosomes for recycling
(3) Receptor-mediated endocytosis: targeted cell ingestion of
extracellular molecules, some of which are destined for the
lysosome (Fig. 7.16)
8. Vacuoles (Fig. 7.17)
a. Vacuoles occupy most of the volume of plant and fungal cells.
b. They act as a storage depot for water, ions, and sometimes
proteins.
c. Plant vacuoles may contain noxious substances that protect the
plant from predators.
9. Mitochondria (Fig. 7.18)
a. Mitochondria are the sites of ATP synthesis.
b. They have two membranes.
(1) The outer membrane is smooth.
(2) The inner membrane contains folds called cristae.
(3) The mitochondrial matrix is inside the inner membrane.
c. Mitochondria contain their own small circular chromosome.
d. They make their own ribosomes and synthesize some proteins.
e. Mitochondria grow and divide independently of cell division.
10. Chloroplasts (Fig. 7.19)
a. Algal and plant cells contain organelles called plastids.

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Freeman, Biological Science, 2Ce, Chapter 7 Instructor Guide − 4

b. Photosynthetic cells contain plastids called chloroplasts, which


convert the energy in sunlight into the chemical energy in sugar.
c. Chloroplasts have two membranes.
(1) The outer membrane is smooth.
(2) The inner membrane is filled with a series of flattened sacs,
called thylakoids, which are stacked in grana.
(3) Thylakoids are surrounded by stroma, the fluid filling the
inner membrane.
d. Chloroplasts have their own DNA and divide independently of
nuclear division.
11. Cell walls (Fig. 7.20)
a. Algal, fungal, and plant cells have cell walls.
b. Cell walls are composed of carbohydrate rods and fibres
running through a stiff polysaccharide and protein matrix.
12. Cytoskeleton (Fig. 7.21)
a. The cytoskeleton is a system of protein fibres.
b. It provides structural support to the cell.
c. It facilitates many types of cellular movement.
III. Putting the Parts into a Whole
A. Structure and function at the whole-cell level (Summary Table 7.2)
1. Examples (Fig. 7.22)
a. Pancreatic cells are specialized for secreting digestive
enzymes. They are packed with RER and Golgi apparatus, the
organelles that manufacture secreted proteins. (Fig. 7.22a)
b. Animal testis cells are specialized for making testosterone, a
steroid hormone. They have an extensive smooth ER network.
(Fig. 7.22b)
c. Plant leaf cells are specialized for absorbing light and
manufacturing sugars. They contain a large number of
chloroplasts. (Fig. 7.22c)
d. Potato tuber cells are specialized for storing sugars. They
contain a large storage vacuole. (Fig. 7.22d)
B. The dynamic cell
1. Light and electron microscopes allow us to see the shapes and
locations of organelles inside a cell.
2. Differential centrifugation allows us to isolate and study the
functions of individual organelles (see BioSkills 11 in Appendix B).
3. Modern imaging techniques allow us to track how the organelles
in a cell act together (see BioSkills 10).
IV. Cell Systems I: Nuclear Transport
A. Structure and function of the nuclear envelope
1. The nucleus is enclosed by a double membrane called the nuclear
envelope. (Fig.7.23a)
a. The outer nuclear membrane is continuous with the rough ER.
b. The space between the inner and outer membranes is
continuous with the lumen of the rough ER.

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2. Nuclear pores penetrate the nuclear envelope and connect the


cytoplasm to the nucleoplasm. (Fig. 7.23b)
a. Nuclear pores consist of 50 different proteins called the nuclear
pore complex.
b. Molecules travel into and out of the nucleus through the nuclear
pores.
(1) rRNA and ribosomal subunits are made in the nucleolus but
are functional in the cytoplasm.
(2) mRNA and tRNA are made in the nucleus but function in
the cytoplasm.
(3) Nucleotide triphosphates, building blocks for DNA and
RNA, and enzymes involved in DNA replication,
transcription, and ribosome assembly are made in the
cytoplasm but function in the nucleus.
B. How are molecules imported into the nucleus?
1. Researchers studying viral proteins noticed that changing a single
amino acid could disable the protein’s ability to enter the nucleus.
2. This observation led to the hypothesis that proteins destined to be
imported into the nucleus contain a nuclear localization signal
(NLS).
3. Experiments using a protein called nucleoplasmin (involved in
chromosome assembly) revealed the nature of the nuclear
localization signal. (Fig. 7.24)
a. What portion of the molecule targets it to the nucleus?
(1) Experimental design: Researchers used enzymes called
proteases to separate the tail region of nucleoplasm from
the head region. They labelled each region with a
radioactive atom and injected them into different living cells.
(2) Results: The researchers found that only the tail regions
were transported into the nucleus.
(3) Conclusion: The tail region contains the nuclear transport
“postal code” tag.
b. Further experiments demonstrated that a 17-amino-acid
stretch of the nucleoplasm in the tail region made up the
nuclear localization signal. Follow-up studies showed that other
proteins have nuclear localization signals that interact with
proteins called importins and exportins, which act as delivery
trucks.
V. Cell Systems II: The Endomembrane System Manufactures and
Ships Proteins
A. Studying the pathway through the endomembrane system (Fig. 7.25)
1. George Palade and his colleagues studied pancreatic cells that
secreted a large volume of proteins in order to understand the role
of the endomembrane system in the production and processing of
secreted proteins.

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2. Secretory pathway hypothesis: The rough ER and Golgi apparatus


form an endomembrane system that directs the production and
secretion of specific proteins.
3. Experimental design: Palade used the pulse-chase technique to
label newly synthesized proteins and visualize them over time.
a. Palade exposed cells to a brief “pulse” of a radioactively
labelled amino acid (leucine).
b. Then he gave the cells a large amount of unlabelled amino
acid (the “chase”).
c. After varying amounts of time, he killed the cells and examined
them under the electron microscope (see BioSkills 9 and 10).
4. Results: The proteins pass from the rough ER to the Golgi
apparatus to secretory granules and are ultimately secreted
outside the cell. (Fig. 7.26)
B. Entering the endomembrane system: the signal hypothesis
1. Günter Blobel and his colleagues hypothesized that proteins
destined to be secreted have a signal in the first few amino acids
that functions as an address tag directing them to the ER.
2. Researchers found that when secreted proteins are synthesized in
a test tube without the ER, they are about 20 amino acids longer
than the same protein that is secreted by cells.
a. When the researchers added ER to their test tubes, the
synthesized proteins were the same length as the endogenous
proteins.
b. The sequence of 20 amino acids is located on the N-terminus
(the beginning) of the protein. It has been named the ER signal
sequence.
3. Recent studies have documented the mechanism by which
proteins with signal sequences are received by and enter into the
rough ER. (Fig. 7.27)
a. A ribosome synthesizes the ER signal sequence, which then
binds to a signal recognition particle (SRP) in the cytoplasm.
b. The ribosome, new polypeptide, and SRP all bind to an SRP
protein receptor on the surface of the rough ER.
c. After binding to the rough ER, the SRP is released, the signal
sequence is removed, and there are two possibilities for the
polypeptide:
(1) The polypeptide may be transferred to the lumen of the ER
so that it can be processed and ultimately packaged into an
organelle or secreted from the cell.
(2) It may be integrated into the rough ER membrane so that it
can be processed and shipped to the plasma membrane.
d. What happens to proteins when they are in the rough ER?
(1) Proteins are folded into their 3D structures with the help of
chaperone proteins.

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(2) Other enzymes modify proteins to glycoproteins by adding


carbohydrate groups (glycosylation). (Fig. 7.28)
C. Moving from the ER to the Golgi
1. Palade and colleagues hypothesized that vesicles bud off of the
ER, move through the cytoplasm to the nearby Golgi apparatus,
fuse with the cis face of the Golgi apparatus, and dump their
contents inside.
2. Studies using electron microscopy combined with differential
centrifugation confirmed this hypothesis and demonstrated that
distinct types of vesicles shuttle materials to the Golgi apparatus.
D. What happens inside the Golgi apparatus?
1. Recent studies have shown that the cisternae in the Golgi are
constantly regenerated by the fusion of vesicles with the cis face
and disposed of as vesicles bud off the trans face.
2. The function of the Golgi is well understood.
a. Cisternae have a different set of enzymes at each stage of
maturation, which catalyze different parts of the glycosylation
reactions.
b. Existing sugar groups on proteins are modified,
phosphorylated, or even removed, while new sugar groups
may be added.
E. How do proteins reach their destinations?
1. Once proteins are manufactured and processed through the ER
and Golgi, they must be sent to the appropriate location or
organelle within the cell.
2. Studies involving lysosomal enzymes reveal that these proteins
are tagged with specific carbohydrate groups (mannose-6-
phosphate) acting as molecular postal codes that target the
proteins to the vesicles destined for the lysosome. (Fig. 7.29)
3. Proteins that are to be secreted are packaged into vesicles
destined for the plasma membrane, where they will fuse and dump
their contents via a process called exocytosis.
4. Proteins that are synthesized in the cytoplasm also have postal
codes directing them to mitochondria, chloroplasts, or other
destinations.
a. The arrays of proteins produced in a cell are sorted via
distinctive postal codes.
b. These molecular address labels allow proteins to be shipped to
the compartment where they function.
VI. Cell Systems III: The Dynamic Cytoskeleton (Summary Table 7.3)
A. Actin filaments
1. Actin filaments or microfilaments are long, fibrous polymers of
globular protein called actin.
a. Actin resembles two long strands twisted together.
b. Actin has polaritya plus end and a minus end; microfilaments
grow at the plus end.

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Freeman, Biological Science, 2Ce, Chapter 7 Instructor Guide − 8

2. Actin filaments form a matrix that helps define the cell’s shape.
3. Actin filaments are also involved in several types of cell movement
that are facilitated by the action of myosin binding to actin
filaments, causing them to slide across one another. (Fig. 7.30)
a. Cell crawling: Extension of actin filaments in one part of the cell
forms pseudopodia that move the cell in a given direction.
b. Cytokinesis: During animal cell division, actin filaments form a
ring beneath the plasma membrane of a dividing cell;
contraction of this ring pinches the cell in two.
c. Cytoplasmic streaming: The directed flow of cytosol and
organelles around plant cells occurs along actin filaments,
powered by myosin.
B. Intermediate filaments (Summary Table 7.3)
1. Intermediate filaments are arranged as fibres wound into thicker
cables.
2. Intermediate filaments called nuclear lamins form a dense network
on the inside of the nuclear envelope that maintains the shape of
the nucleus.
3. Intermediate filaments also form a flexible skeleton between the
nucleus and the rest of the cell that helps the nucleus stay in
place.
C. Microtubules
1. Microtubules are composed of tubulin dimers that polymerize to
form a hollow tube that has polarity (a plus end and a minus end).
2. Microtubules move and separate chromosomes during mitosis.
a. Microtubules originate from a structure called the microtubule-
organizing centre (MTOC) and grow outward to radiate
throughout the cell.
b. In animals, the MTOC is called a centrosome. (Fig. 7.31)
Animal centrosomes contain two bundles of microtubules
called centrioles.
c. Canadian Research 7.2: Pathogenic bacteria alter the
cytoskeleton of human cells. (Fig. 7.32)
3. Microtubules act as “railroad tracks.” (Fig. 7.34)
a. Ronald Vale and colleagues studied how vesicles move
throughout the cell by using the extruded cytoplasm of a squid
giant axon.
(1) They found that vesicle transport occurred along a
filamentous track in the cytoplasm and that vesicle
transport requires the presence of ATP.
(2) They found that vesicle transport was abnormal when
microtubule-disrupting drugs were added to the
preparation.
(3) The researchers concluded that vesicle transport was
occurring along microtubules and required the energy from
the hydrolysis of ATP.

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4. A motor protein generates motile forces.


a. Vale went on to identify the means by which a vesicle moves
along a microtubule.
(1) Kinesin is a motor protein that contains three major regions:
a head region with two globular pieces, a tail associated
with small polypeptides, and a stalk that connects the head
to the tail. (Fig. 7.35a)
(2) The globular pieces on the head contain microtubule
binding sites as well as ATP binding sites; the tail region
can bind the transport vesicle.
(3) Kinesin walks along the microtubule when the head region
binds to ATP. (Fig. 7.35b)
D. Flagella and cilia: moving the entire cell
1. How are cilia and flagella constructed? (Fig. 7.37)
a. Cilia and flagella have nine pairs of microtubules that surround
two individual microtubules. This “9 + 2” structure is called an
axoneme. (Fig. 7.37a)
b. The axoneme attaches to the cell at the basal body, a structure
identical to a centriole.
c. Electron microscopic studies revealed that the nine
microtubule pairs are connected by motor proteins called
dynein, and the centre microtubules are connected to the nine
doublets by protein spokes. (Fig. 7.37b)
2. What provides the force required for movement?
a. Dynein hydrolyzes ATP and changes shape, thus “walking”
along in a manner similar to that of kinesin.
b. This walking causes the microtubules within the cilia or flagella
to slide past one another.
c. However, this sliding is limited because the whole structure is
anchored to the centre microtubules by the protein spokes.
d. This constrained movement results in the bending of the cilia
or flagella, thus creating movement. (Fig. 7.38)

Chapter Vocabulary

plasma membrane cytoplasm rough endoplasmic


morphology organelle reticulum (RER)
phylogeny cytoskeleton lumen
chromosome flagellum smooth endoplasmic
prokaryote cell wall reticulum (SER)
eukaryote glycolipid Golgi apparatus
gene nucleus cisterna
nucleoid nuclear envelope cytosol
plasmid nuclear lamina perixosome
ribosome nucleolus glyoxysome

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lysosome differential cytokinesis


autophagy centrifugation cytoplasmic
phagocytosis nuclear pore streaming
receptor-mediated nuclear pore cell crawling
endocytosis complex intermediate filament
early endosome nuclear localization nuclear lamin
late endosome signal (NLS) microtubule
endocytosis secretory pathway dimer
pinocytosis hypothesis microtubule
endomembrane pulse-chase organizing centre
system experiment (MTOC)
vacuole culture centrosome
mitochondrion ER signal sequence centriole
crista signal recognition pathogenic
mitochondrial matrix particle (SRP) kinesin
plastid glycosylation cilium
chloroplast glycoprotein axoneme
thylakoid exocytosis basal body
granum microfilament dynein
stroma actin filament
motor protein

Lecture Activities

Case Study: Asbestosis


Estimated duration of activity: 15+ minutes
Case studies are an excellent way to increase student interest in biology.
This exercise may be done completely in class (if the class or a discussion
section can meet in a computer lab), or it may be started in class and
finished as an out-of-class assignment. It may also be assigned as
homework and discussed during the next class session.
This case study guides students to investigate the important roles that
lysosomes play in human cells and to understand the consequences of
lysosomal dysfunction.
Procedure:
1. After dividing the students into groups, hand out the first part of the case
study; ask them to brainstorm and make a list of questions about the
case.
2. Have each group come up with one or two questions that will be
assigned to each group member for part 1 (see the following part
descriptions).
3. After the lists are complete (this should take about 10 minutes), give the
groups part 2; have students add to their lists and revise their questions
from part 1.

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4. Repeat for parts 3 and 4. By the end of the class period, each group
should have formulated a list of questions that can be divided among the
group members.
5. Group members must then find the answers to their questions. As
information sources, encourage them to use the Internet (reputable,
referenced sources only), their textbook, other textbooks, scholarly
journals, and so on. You may want to have them bring their information to
the next class, allowing groups to meet again to finish the assignment.
6. Alternatively, students may report to each other by e-mail (or on a class
website) and then write individual responses to the assignment.
7. As a third alternative, you may choose to do this exercise quickly as a
class. In this case, you may provide all the answers to the brainstorming
group questions. This approach allows the students to reach a
conclusion by the end of class but does lose the self-directed research
aspect of the exercise.
Part descriptions:
• Part 1: Chuck hasn’t been feeling well lately. He is often out of breath, his
chest feels tight, and he isn’t eating much. But, worst of all, he is
constantly coughing up mucus.
• Part 2: Chuck has worked for American/Atlantic Construction Company
for 25 years. They are renovation specialists who restore old office
buildings. Chuck is on the team that removes the old asbestos-containing
insulation in the buildings, replacing it with asbestos-free insulation.
Chuck likes his job, but he hates the protective suits he must wear while
removing the old insulation. He much preferred the early years with the
company, when they didn’t have to wear all that stuff! The company says
the suits are protection against asbestos. Chuck doesn’t understand the
big fuss about asbestos. He can’t see it, so how could it possibly hurt
him?
• Part 3: Chuck goes to the doctor and describes his symptoms. The
doctor listens to his chest and says he can hear a crackling sound when
Chuck breathes. He also has Chuck breathe into an instrument and then
comments that Chuck has very low tidal volume. Last, the doctor orders
chest X-rays and, after reviewing them, tells Chuck that he has found
bilateral calcified plaques in the lower quadrant of the lungs as well as
several irregular opacities in the same regions.
• Part 4: You are a health-care representative for the union that Chuck
belongs to. Chuck is overwhelmed by medical bills and is contacting you
to see whether he has a valid case to claim this condition on the
company’s worker’s compensation program. Chuck has not yet gotten a
diagnosis from his doctor, but he hopes that you can help him figure out
what is going on and what caused this problem. He hopes that you can
explain to him what is happening. Compose an e-mail to Chuck covering
these questions: What is wrong with Chuck? Which specific organ is
affected by this ailment? What is happening in the affected cells? What
caused this ailment? What are the treatment and prognosis for this

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ailment? Do you think this is a valid claim for worker’s compensation? Do


you think the company was at fault, or was Chuck?
Internet resources:
www.mayoclinic.com/health/asbestosis/DS00482
www.nlm.nih.gov/medlineplus/ency/article/000118.htm

Think, Pair, and Share


Estimated duration of activity: 20–25 minutes
Toward the end of Chapter 7, pose the following question to the students to
Think about in preparation for the next class. In the next class, have them
form groups, or Pair with each other, and discuss their thoughts on the
question. Then, ask each group to Share their thoughts with the entire class.
The question is: Eukaryotic cells are generally about 1000 times the size of
prokaryotic cells. What are the structures and mechanisms that evolved in
eukaryotic cells that enabled them to become so much larger than
prokaryotic cells? Tell the students there are at least two major differences
between the two types of cells that account for their size difference.
Here are the answers that should come out by the end of the
discussion:
1. Prokaryotes have only one membrane surrounding each cell. This limits
the size of the cell because the cell’s internal volume cannot be so large
that the force of diffusion is unable to move a molecule from the outside
of the cell to the centre of the cell. If the distance from the cell surface to
the centre of the cell becomes too large, molecules will not be able to
diffuse into the centre of the cell because diffusion is a local force that
cannot move molecules great distances.
2. Eukaryotic cells, in contrast, have evolved many internal membrane-
bound organelles. All of those membranes count as part of the total
surface area of the cell. Therefore, the distance from one membrane to
another is never so great as to prevent the force of diffusion from moving
a molecule.
3. The first two answers are part of the one major difference the students
need to identify. The other difference is how molecules are moved
around in the eukaryotic cell—packaged in vesicles traveling on the
fibres of the cytoskeleton. This is directed motion, powered by the
hydrolysis of ATP. Thus, the expenditure of energy allows the cell to
overcome the limitations of the force of diffusion.
Exercise objectives:
• Review the relevant portions of Chapter 7 that cover the internal structure
of prokaryotic and eukaryotic cells.
• Compare and contrast those structures.
• Come up with ideas that address the question.
• Participate in class discussions that further the entire class’s
understanding of the topic.

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Procedure:
1. Ask students to review Chapter 7 and compare eukaryotic cell
structures with prokaryotic cell structures.
2. Ask students to think about the question and then write down their
responses, issues, and additional questions that are relevant.
3. Ask students to bring their written ideas to class and then form groups
to discuss their ideas. At the end of the class period, collect each
student’s written ideas. The written ideas should be evaluated in a
formative way, as should anything collected from this exercise. The
evaluation should be just a check mark to indicate that the exercise
was done. Provide students with helpful comments to consider for the
next time this type of exercise is attempted.
4. The groups must discuss each person’s idea(s), refine the ideas, and
then write down the answers the group is most comfortable with.
Collect these ideas for a formative assessment. The discussion
should be limited to 10–15 minutes.
5. The groups should then informally share their ideas with the rest of
the class. After each group has spoken, say something like, “What
does everybody think about the other groups’ ideas? Are any of the
ideas really good? Are there any ideas we can develop further?”

Survey on Think, Pair, and Share Activity


Name (optional) _____________________
Course/section # _____________________
Date of the discussion: _____________________
1. How much time did you spend on your own thinking about the
question for discussion?
2. How much time did you spend discussing the question with your
group?
3. How well did the group discussion go for you? Did you feel you made
your opinion known? Did you feel your opinion was carefully
considered by the group?
4. How well did you think the class discussion went?
5. Overall, how much did you get out of this exercise?
6. Any other comments?

In-Class Demonstration: Pulse-Chase Experiment


Estimated duration of activity: 5 minutes as you are lecturing, then 3–5
minutes to explain the demonstration
This activity is rather elementary but will give the students a fun way to
visualize how a pulse-chase experiment works. Because so many students
are visual learners, role-playing demonstrations are often a fun and visual
way to help them understand dynamic biological processes. Even the
brightest students will at least appreciate the break from lecture.

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After or during an explanation of the pulse-chase experiment and its


usefulness in visualizing molecule movement in a cell, perform the following
demonstration.
Purpose: Tell students they are going to create a pathway that you will be
able to define without knowing it ahead of time (even the students won’t
know the pathway because it is created as the demonstration progresses)
and without watching the pathway directly.
Instructions to students: Tell students that when they are handed a piece of
paper (different-coloured sticky notes work well), they must discreetly hand it
to a nearby student of their choosing. The main rule is that each student
must always hand every note they are given to the same nearby student.
They must pass their note along only when they receive a new note. Instruct
them to end the “pathway” after a reasonable number of students have
become involved; the self-designated “end” person may accumulate the
sticky notes. Instruct students to temporarily stop passing when you say
“Data collection.” At that time, only the people holding pink notes should hold
them up. You can then say “Resume” to indicate that they can start passing
notes again.
Logistics: Start the demonstration by handing a student in the front row a
yellow note (it works better when a student or a teaching assistant does this,
so the instructor can turn his/her back or simply lecture without paying
attention to where the notes are going). Ask the students to wait several
seconds before passing the note along. After they have given their note
away, keep handing that first student yellow notes and have him/her pass
them along. After the 10th note or so, begin handing the first student pink
notes. After handing out five or six pink notes, switch back to yellow. (The
pink is your “pulse” and the yellow is your “chase.”) When you “collect data,”
record the position of the students holding pink papers. After several cycles
of data collection, you should be able to map the pathway that the students
have created.
Analogies: The classroom represents the interior of the cell, and the
students represent an organelle system (the endomembrane system or the
cytoskeleton, for example). The sticky notes represent molecules: The pink
notes are labelled molecules that form the pulse, and the yellow notes are
the chase of unlabelled molecules. The data-collection periods represent the
method researchers use to “stop” different samples in order to visualize
where the label is at different times after the pulse has been initiated.

Discussion Idea
After discussing protein synthesis and modification through the
endomembrane system, ask your students the following questions: How are
proteins sorted into vesicles? How are those vesicles targeted to the
appropriate destination? Then ask students to develop one or more
hypotheses, and ask them what experiments they might perform to test their
hypotheses. Describe the experimental design performed by Lippincott-
Schwartz and her colleagues. Describe each experiment and review each

 2014 Pearson Canada, Inc.


Freeman, Biological Science, 2Ce, Chapter 7 Instructor Guide − 15

data figure, pointing out the pertinent points. As you look at each figure, ask
a student to summarize each experiment and record the data on the board.
When all of the data have been recorded, ask the students to summarize the
major findings of the paper. Then use their conclusions to segue into
discussing Figure 7.29, the current model for how proteins are sorted into
distinct vesicles and targeted to the appropriate destination.
Note: This activity will work best in a classroom that is outfitted with
computer projection and an Internet connection, or in a computer lab.Presley
et al. 1997. ER-to-Golgi transport visualized in living cells. Nature. 389: 81-85.

 2014 Pearson Canada, Inc.

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