Cell Bio Final_Exam 2_2019 Flashcards
- What accounts for the differences in function between the types of ER?
1) The location of the ER
2) The proximity of the ER to the nucleus
3) The protein content of the ER
4) The shape of its component lipids
C: 3
- Which of the following is NOT a function associated with the smooth endoplasmic reticulum in at least some cells?
A. Synthesis of steroid hormones
B. Detoxification of many organic compounds, like barbiturates and ethanol
C. Synthesis of some kind of lipid
D. Synthesis of integral protein
E. Sequestration of calcium Ca2+ ions within the cisternal space
D: Synthesis of integral protein
- What is the arrangement of organelles in a secretory cell from the basal end to the apical end, an arrangement that reflects the flow of secretory products from synthesis to discharge?
A. Golgi complex- nucleus and RER- secretory vesicles
B. Nucleus and RER- Golgi complex- secretory vesicles
C. Nucleus and RER- secretory vesicles- nucleus and RER
D. Golgi complex- secretory vesicles- nucleus and RER
E. Secretory vesicles- nucleus and RER- Golgi complex
B: Nucleus and RER- Golgi complex- secretory vesicles
- What are the two sites within a cell at which protein synthesis is generally thought to occur?
A. Cytosolic surface of RER and cisternal surface of RER
B. Cytosolic surface of RER and free ribosomes
C. Cisternal surface of RER and free ribosomes
D. Free ribosomes and cytosolic surface of RER
E. Cytosolic surface of RER and cytosolic surface of SER
B: Cytosolic surface of RER and free ribosomes
- Blobel, Sabatini, and Dobberstein proposed that the site of protein synthesis is determined by information contained in the N-terminal portion of the protein, the first part to emerge from the ribosome. What did they call their proposal?
D: The signal hypothesis
6. What effect does the binding of SRP to the growing polypeptide chain and the ribosome have on protein synthesis? A. Protein synthesis accelerates B. Protein synthesis ceases temporarily C. Protein synthesis ceases permanently D. Protein synthesis is terminated E. The ribosome dissociates
B: Protein synthesis ceases temporarily
- Why is the ER so well-suited and ideally constructed for its role as a port of entry for secretory proteins?
1) It has a large surface area allowing the attachment of many ribosomes.
2) The ER cisternae lumen favors folding and assembly of proteins.
3) The RER can segregate secretory, lysosomal and cytoplasmic proteins from other newly made proteins, allowing their modification, and sends them to their final destination
D: 1 and 2
- How are integral membrane proteins thought to enter the lipid bilayer?
A. They insert into the membrane from the RER lumen after their synthesis is complete.
B. The aqueous translocon channel seems to have a gate that continuously opens and closes, giving each nascent polypeptide segment a chance to partition itself into the lipid bilayer’s hydrophobic core.
C. They insert into the membrane from the cytosol after their synthesis is complete.
D. It is thought that they burrow into the lipid bilayer.
E. It is thought that they are enzymatically implanted in the lipid bilayer.
B: The aqueous translocon channel seems to have a gate that continuously opens and closes, giving each nascent polypeptide segment a chance to partition itself into the lipid bilayer’s hydrophobic core.
- How and where is the asymmetry of the phospholipid bilayers initially established?
A. It is initially established in the Golgi complex during lipid and protein modification
B. It is initially established in the ER during lipid and protein synthesis
C. It is initially established in the secretory vesicles during lipid and protein modification
D. It is initially established in the mitochondria by random insertion into the membranes
E. All of these are correct
B: It is initially established in the ER during lipid and protein synthesis
10. To what residue of a polypeptide are N-linked oligosaccharide chains attached as that polypeptide enters the RER lumen through the translocon? A. Arginine B. Asparagine C. Serine D. Threonine E. Ninhydrin
B: Asparagine
- How do protein coats select the cargo molecules to be carried by the vesicles they help to form?
A. They electromagnetically attract the correct cargo proteins
B. The protein coats have a specific affinity for the cytosolic tails of integral membrane proteins that reside in the donor membrane
C. The coats have a specific affinity for the luminal tails of integral membrane proteins that reside in the donor membrane
D. The coat proteins directly attach to the cargo proteins in the lumen of the forming vesicles
E. The coat proteins attach to the extracellular matrix
B: The protein coats have a specific affinity for the cytosolic tails of integral membrane proteins that reside in the donor membrane
- The coat vesicles that transport materials around the cell interior __________.
1) Is composed of two distinct protein layers
2) Possesses an outer cage or scaffolding that forms the framework for the coat
3) Possesses adaptors that are able to select specific cargo molecules
4) Possesses an inner layer of adaptors that serves primarily to bind the vesicle’s cargo
A. 1 + 2 + 4
B. 2 + 3 + 4
C. 1 + 3 + 4
D. 1 + 2 + 3
E. 1 + 2 + 3 + 4
E: 1 + 2 + 3 + 4
13. What would happen to the movement of vesicles toward their eventual target if a microtubule inhibitor, which can prevent assembly of the microtubule, were added to the cells? A. The vesicles would disintegrate B. The vesicles would move faster C. Vesicle movement would slow or stop D. Vesicles will shrink E. Vesicles will swell
C: Vesicle movement would slow or stop
14. Which of the following enzymes are typically found in lysosomes? A. Hydrolytic enzyme (acid hydrolases) B. Oxidoreductases C. Transferases D. Lyases E. Ligases
A: Hydrolytic enzyme (acid hydrolases)
- What is thought to shield lysosomal membranes against attack by their enclosed enzymes?
A. DNA
B. Basic RNA
C. Carbohydrate chains attached to integral membrane proteins
D. Carbohydrate chains attached to peripheral membrane proteins
E. The lipid bilayer itself
C: Carbohydrate chains attached to integral membrane proteins