Cell Biology Questions and Answers – Gene Expression Control – Post-translational Control

This set of Cell Biology Multiple Choice Questions & Answers (MCQs) focuses on “Gene Expression Control – Post-translational Control”.

1. Degradation of cellular unwanted proteins is carried out in _________
a) Proteasomes
b) Lysosome
c) Peroxisomes
d) Ribosomes
View Answer

Answer: a
Explanation: Cellular proteins are degraded in the proteasomes.They are made up of 2 different protein complexes(two α subunit and two β subunit). Lysosomes however degrade extracellular proteins and other macromolecules.
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2. How many β-subunits are there in proteasomes?
a) 2
b) 3
c) 4
d) 5
View Answer

Answer: a
Explanation: In proteasomes, there are four polypeptide rings stacked one on top of the other and a cap attached at either side of the stack. The two central rings are β-subunits are the main site for proteolysis.

3. Proteins that terminate in arginine are short-lived.
a) True
b) False
View Answer

Answer: a
Explanation: Although exact factors that determine the longevity of a protein are not yet clear. One of the determinants is amino acid sequence at the N-terminus of the polypeptide. Polypeptides that terminate in arginine and lysine are short-lived.

4. “Degron” is a __________
a) enzyme
b) polypeptide
c) amino acid sequence
d) nucleic acid sequence
View Answer

Answer: c
Explanation: For post-translational control, it is important that regulatory proteins are degraded in time. Certain proteins contain a specific internal amino acid sequence in their polypeptide chain, that ensure timely degradation.
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5. Ubiquitin is a ___________________
a) protein
b) organelle
c) nuclear body
d) aggragated complex
View Answer

Answer: a
Explanation: Ubiquitin is an important protein that performs functions in diverse cellular processes. It is a small and highly conserved protein. A single attached ubiquitin can serve as a sorting signal leading the associated polypeptide to a specific pathway.

6. A number of ubiquitin molecules must be attached to ensure enzymatic degradation of a polypeptide.
a) True
b) False
View Answer

Answer: a
Explanation: A single attached ubiquitin functions as a sorting signal while for ensuring enzymatic degradation of polypeptides, a number of ubiquitin molecules must be enzymatically transferred to the polypeptide.

7. For enzymatic degradation, Ubiquitin is transferred from the carrier protein to _______________ residue.
a) arginine
b) cytosine
c) lysine
d) alanine
View Answer

Answer: c
Explanation: Ubiquitination is the process of adding ubiquitin molecules to damaged or old proteins. The last Amino acid of ubiquitin is attached to a lysine residue on the substrate protein.
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8. Which part of the proteasome recognizes a polyubiquitinated protein?
a) alpha-subunit
b) beta-subunit
c) gamma-subunit
d) end caps
View Answer

Answer: b
Explanation: Once the protein is polyubiquitinated, it is ready for enzymatic degradation by the proteasome. The cap of proteasome recognizes the protein and removes the ubiquitin chain and unfolds the target protein.

9. In the proteasome, the unfolded protein is threaded through narrow opening in the ring of ___________________
a) ligase
b) sigma factor
c) alpha-subunit
d) beta-subunit
View Answer

Answer: c
Explanation: In the proteasome after removal of ubiquitin chain the unfolded linear peptide moves through the narrow opening in the rings of alpha-subunits and passed to the central chamber where degradation takes place.

Sanfoundry Global Education & Learning Series – Cell Biology.

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Manish Bhojasia, a technology veteran with 20+ years @ Cisco & Wipro, is Founder and CTO at Sanfoundry. He is Linux Kernel Developer & SAN Architect and is passionate about competency developments in these areas. He lives in Bangalore and delivers focused training sessions to IT professionals in Linux Kernel, Linux Debugging, Linux Device Drivers, Linux Networking, Linux Storage, Advanced C Programming, SAN Storage Technologies, SCSI Internals & Storage Protocols such as iSCSI & Fiber Channel. Stay connected with him @ LinkedIn | Instagram | Facebook | Twitter