#Question id: 4284
#Unit 3. Fundamental Processes
Assays for following the trafficking of proteins through the secretory pathway in living cells require
a. sensitive methods to distinguish the very small differences in organelle density caused by passage of a wave of protein transport through the organelle.
b. a way to identify compartments where labeled proteins are located.
c. the use of cell types that are highly dedicated secretory cells.
d. the use of enucleate cells in order to eliminate the nucleus as a site of labeling.
e. a way to label a cohort of secretory proteins
#Question id: 4285
#Unit 3. Fundamental Processes
VSV G protein has been a very useful tracker protein for both living cell and in vitro assays because
#Question id: 4286
#Unit 3. Fundamental Processes
Transport vesicles
a. can have a clathrin coat. b. can be coated with a heteromeric COPI and COPII coat.
c. can contain assembly proteins.
d. can shuttle proteins from mitochondria to the endoplasmic reticulum.
e. can fuse with target organelles.
#Question id: 4287
#Unit 3. Fundamental Processes
How the mTOR pathway increases the protein synthesis?
#Question id: 4288
#Unit 3. Fundamental Processes
During eukaryotic protein synthesis, stress conditions result in activation of specific kinases leading to phosphorylation of a key translation initiation factor that inhibits protein synthesis from a large number of cellular mRNA. Which one of the following factors is the kinase?
#Question id: 4289
#Unit 3. Fundamental Processes
Match the Following
|
A. fidelity of codon recognition |
1. involves two adjacent adenine residues in the 16S rRNA component located within the A-site of the small subunit. These bases form hydrogen bonds with the minor groove of each correct base pair formed between the anticodon and the first two bases of the codon in the A-site |
|
B. kinetic selectivity |
2. Even a single mismatch in the codon–anticodon base pairing alters the position of EF-Tu, reducing its ability to interact with the factor-binding center. This, in turn, leads to a dramatic reduction in EF-Tu GTPase activity |
|
C. Accommodation |
3. When the charged tRNA is first introduced into the A-site in a complex with EF-Tu-GTP, its 30 end is distant from the site of peptide-bond formation. To participate successfully in the peptidyl transferase reaction, the tRNA must rotate into the peptidyl transferase center of the large subunit in a process |