#Question id: 4293
#Unit 3. Fundamental Processes
Match antibiotics with their effects
A. Tetracycline |
1. Inhibits aminoacyl-tRNA binding to A-site in prokaryotes |
B. Chloramphenicol |
2. Blocks correct positioning of A-site aminoacyl-tRNA for peptidyl transfer reaction in prokaryotes |
C. Fusidic acid |
3. Prevents release of EF-G–GDP from the ribosome in prokaryotes |
D. Ricin |
4. Prevents activation of translation factor GTPases in both Prokaryotes and Eukaryotes |
#Question id: 4294
#Unit 3. Fundamental Processes
Not surprisingly, in several instances, the two binding sites for the regulatory ribosomal protein are related to each another. In the case of the S8 ribosomal protein, the two binding sites share substantial similarities. The sequence of the binding site in the mRNA reveals a clear mechanism by which S8 inhibits translation. Which of the following are INCORRECT regarding this mechanism?
A. Free rRNA content in cytoplasm activates ribosomal protein biogenesis
B. RNA-binding proteins regulate their expression by binding to their own mRNAs, including some aminoacyl-tRNA synthetases
C. In case of “NO FREE rRNA” ribosomal protein transcript is efficiently translated by autoregulation process
D. In case of “NO FREE rRNA” ribosomal protein transcript undergoes to autorepression
#Question id: 4295
#Unit 3. Fundamental Processes
Regulating iron levels in the human body is critical. Many proteins use iron as a cofactor, including the oxygen transport proteins hemoglobin and myoglobin. Consistent with the important role of iron in oxygen transport and energy production, a shortage of iron in the human body (called anemia) results in an overall feeling of weakness. On the other hand, excess iron is toxic to cells and can contribute to liver damage, heart failure, and diabetes. The iron-binding protein Ferritin is the major regulator of iron levels in the human body. Which of the following are INCORRECT regarding ferritin?
A. Ferritin translation is regulated by iron-binding proteins called iron regulatory proteins
B. The levels of transferrin, transferrin receptor, are also crucial to cellular iron homeostasis
C. Aconitase regulates synthesis of these three proteins is regulated in response to iron availability
D. apoaconitase, is actually IRE that has ability to bind to specific sequences in the mRNAs for the transferrin receptor and ferritin, thus regulating protein synthesis at the translational level.
E. IRE binding to mRNA increases synthesis of ferritin many folds.
#Question id: 4296
#Unit 3. Fundamental Processes
Normally, a stop codon is required to release the ribosome from an mRNA but what happens to a ribosome that initiates translation of an mRNA fragment that lacks a termination codon. The Ribosome stalled at broken part of mRNA. In prokaryotic cells, such stalled ribosomes are rescued by the action of a chimeric RNA molecule that is part tRNA and part mRNA, appropriately called a tmRNA. What is sequence of events of this rescue process.
A. Translocation of the peptidyl-SsrA RNA results in the release of the broken mRNA
B. the SsrAAla–EF-Tu–GTP complex binds to the A-site of the ribosome and participates in the peptidyl transferase reaction
C. portion of the SsrA RNA acts as an mRNA and encodes 10 codons followed by a stop codon
D. the protein encoded by the incomplete mRNA is fused to a 10-amino-acid “peptide tag” at its carboxyl terminus, and the ribosome is recycled. Interestingly, the 10-amino-acid tag is recognized by cellular proteases that rapidly degrade the tag and the truncated polypeptide to which it is attached
#Question id: 4297
#Unit 3. Fundamental Processes
Match the following decay mechanism
A. Matured translation |
1. Ribosome displaces all of the exon–junction complexes. |
B. nonsense-mediated mRNA decay |
2. Upf complex |
C. nonstop-mediated decay |
3. eRF1 and eRF3 |
D. no-go decay |
#Question id: 4298
#Unit 3. Fundamental Processes
Insulin and other growth factors stimulate a pathway involving a protein kinase mTOR, which in its turn augments protein synthesis. mTOR essentially modifies protein(s) which in their unmodified form act as inhibitors of protein synthesis. The following protein is NOT possible candidate: