GRE Subject Test: Biochemistry, Cell, and Molecular Biology : GRE Subject Test: Biochemistry, Cell, and Molecular Biology

Study concepts, example questions & explanations for GRE Subject Test: Biochemistry, Cell, and Molecular Biology

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All GRE Subject Test: Biochemistry, Cell, and Molecular Biology Resources

1 Diagnostic Test 201 Practice Tests Question of the Day Flashcards Learn by Concept

Example Questions

Example Question #2 : Help With Protein Degradation

Ubiquitination of a protein is one way to mediate protein degradation, however, ubiquitination is only a signal. What is ultimately responsible for ubiquitin-mediated degradation of a protein?

Possible Answers:

Proteasome

Peroxisome

Hydrolysis

None of these

Lysosome

Correct answer:

Proteasome

Explanation:

The correct answer is proteasome. Ubiquitination of a protein signals for the proteasome to degrade it and recycle the ubiquitin. Alternatively, the lysosome does degrade proteins, however, this process is independent of ubiquitin. The peroxisome is responsible for the degradation of fatty acids, certain amino acids, and reactive oxygen species. Hydrolysis simply refers to a chemical mechanism that splits apart a compound by the addition of water, it does not however, describe an organelle or cellular compartment that is reponsible for protein degradation. 

Example Question #33 : Cellular Processes

The ubiquitin-mediated protein degradation process targets proteins to which cellular structure for degradation? 

Possible Answers:

Lysosome 

Endoplasmic reticulum

Golgi

Vesicle 

Proteasome

Correct answer:

Proteasome

Explanation:

The correct answer is proteasome. There are two general protein degradation processes: the first involving the lysosome and the second involving the proteasome. Lysosomal protein degradation is non-selective and occurs during cell starvation. Degradation through the proteasome is dependent on ubiquitination of the target protein, and as such, ensures protein-specific degradation. 

Example Question #3 : Help With Protein Degradation

How does ubiquitination of a protein facilitate its degradation? 

Possible Answers:

Promotes exocytosis of the protein

Promotes reprocessing through the Golgi apparatus

None of the other answers 

Recognition of ubiquitin by the lysosome

Recognition of ubiquitin by the proteasome

Correct answer:

Recognition of ubiquitin by the proteasome

Explanation:

The correct answer is recognition of ubiquitin by the proteasome. Ubiquitin-mediated protein degradation by the proteasome is a well characterized method of specific protein degradation. The protein targeted for degradation is phosphorylated, then ubiquitinated. The proteasome recognizes these distinct ubiquitin chains and degrades the protein. Protein degradation can also occur through the lysosome, but this is independent of ubiquitination and is less specific. The golgi complex is involved in protein folding and modification of recently translated amino acid chains. 

Example Question #35 : Cellular Processes

What is the difference between proteolysis and ubiquitin-mediated protein degradation? 

Possible Answers:

Proteolysis is the degradation of organelles whereas proteins are degraded through ubiquitin-dependent mechanisms

Proteolysis occurs in the lysosome but ubiquitin-mediated protein degradation is in the proteasome

Proteolysis occurs in only in the nucleus, but ubiquitin-mediated protein degradation occurs only in the cytoplasm

These two processes are synonymous 

Correct answer:

Proteolysis occurs in the lysosome but ubiquitin-mediated protein degradation is in the proteasome

Explanation:

The correct answer is that proteolysis occurs in the lysosome but ubiquitin-mediated protein degradation is in the proteasome. Proteolysis-lysosomal degradation is non-selective and is activated upon cellular starvation. ubiquitin-mediated protein degradation is highly specific and functions to promote a wide range of cellular processes. 

Example Question #3 : Help With Protein Degradation

Which of the following additions to a protein will signal the cell to degrade it?

Possible Answers:

Ubiquitination

Hydroxylation

Glycosylation

Glycation

Correct answer:

Ubiquitination

Explanation:

Older proteins in our bodies need to be degraded once they become damaged or no longer necessary. One way that the cell tags these proteins is by adding a ubiquitin tag, which can then be recognized by a proteasome, leading to the proteins' deconstruction.

Example Question #1 : Help With Vesicle Transport

Which of the following protein coats would most likely be seen on a vesicle directed towards the plasma membrane?

Possible Answers:

COPII

None of the answers

COPI

Clathrin

Correct answer:

Clathrin

Explanation:

Clathrin coats are often seen trafficking vesicles from the Golgi apparatus to the plasma membrane. Clathrin protein is used to facilitate membrane invagination and vesicle formation, as well as direct vesicle release.

COPI coats are seen in vesicles headed from the Golgi apparatus back to the endoplasmic reticulum. COPII coats are seen in vesicles headed towards the Golgi apparatus from the endoplasmic reticulum.

Example Question #11 : Protein Regulation

Which of the following portions of the cytoskeleton are used extensively for vesicular transport?

I. Actin

II. Intermediate filaments

III. Microtubules

Possible Answers:

I, II, and III

III only

I and III

I and II

Correct answer:

I and III

Explanation:

Actin and microtubules have similar chemical properties. They maintain a nucleotide gradient (ADP/ATP for actin and GDP/GTP for microtubules) across their structures and have two distinct polarized ends. Intermediate filaments do not have either of these characteristics. For that reason, motor proteins associate with actin and microtubules as opposed to intermediate filaments. The polarity of the microtubules and actin allow the motor proteins to become oriented, transporting cargo in a particular direction along the structure. These motor proteins (such as myosin, dynein, and kinesin) are essential for vesicular transport.

Example Question #2 : Help With Vesicle Transport

Which of the following proteins/structures are involved in the mechanism of vesicular transport?

I. Actin microfilament cytoskeleton

II. Intermediate filament cytoskeleton

III. Kinesin

IV. Microtubule cytoskeleton

Possible Answers:

III and IV

I and II

II only

I, III, and IV

Correct answer:

I, III, and IV

Explanation:

Both the actin microfilament cytoskeleton and the microtubule cytoskeleton serve important functions in vesicular transport. They serve as the structures upon which motor proteins move, essentially providing a directional tract for vesicular transport. Motor proteins, such as kinesin, associate with vesicles and bring them from one area of the cell to the other along the directional filaments.

The intermediate filament cytoskeleton lacks the polarity displayed by actin microfilaments and microtubules, making it not very useful for vesicular transport.

Example Question #1 : Help With Vesicle Transport

Botulinum toxin is a neurotoxin that causes paralysis of the muscles. This is accomplished by cleavage of SNARE proteins contained within the presynaptic compartment of the neuron. Given this information, which of the following best describes how botulinum toxin causes paralysis? 

Possible Answers:

Cleavage of SNAREs inhibits vesicles containing neurotransmitters from fusing to the membrane and stimulating the post-synaptic muscle

Disruption of SNAREs reverses transport of vesicles to a retrograde direction, taking them away from the muscle and towards the cell soma

Cleavage of SNAREs disrupts the propagation of the action potential from the axon hillock to the presynaptic membrane

The toxin prevents the SNAREs from stimulating proper synthesis of neurotransmitters in the neuron

The toxin is globally toxic and the organism is paralyzed as the tissue becomes necrotic

Correct answer:

Cleavage of SNAREs inhibits vesicles containing neurotransmitters from fusing to the membrane and stimulating the post-synaptic muscle

Explanation:

This requires knowing that SNARE proteins are required for proper vesicle fusion to the membrane, thereby permitting exocytosis of neurotransmitters into the synaptic cleft and activating the next target; muscle in this case. Paralysis comes because the muscle is not receiving any input once the toxin has cleaved/destroyed the SNARE proteins. 

Example Question #1 : Help With Vesicle Transport

Which of the following motor proteins carries vesicular cargo along microtubules exclusively towards the microtubule organizing center (MTOC)?

Possible Answers:

Dynein

Myelin

Actin

Microfilament

Kinesin

Correct answer:

Dynein

Explanation:

Actin (microfilaments) is a cytoskeletal component, and myelin is an axon wrapping component; not molecular motors. Kinesin is a motor that moves in the plus-end direction, away from the MTOC. Dynein is the correct answer; it moves in the minus-end direction towards the MTOC.

All GRE Subject Test: Biochemistry, Cell, and Molecular Biology Resources

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