Non-muscle contractile bundles are regulated by: 

#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

#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:

#Question id: 4299

#Unit 3. Fundamental Processes

Lactate dehydrogenase (LDH) can exist as various tetrameric isozymes. Extracts from different rat tissues were run on a nondenaturing polyacrylamide gel and stained for LDH activity, as shown below. Standard tetramers of M subunits (M4) and H subunits (H4) were run alongside the tissue extracts. Which of the following is the subunit composition of the isozyme running at position 2 ?

#Question id: 4300

#Unit 3. Fundamental Processes

Find correct order of cotranslational translocation in endoplasmic reticulum

A. Transfer of the nascent polypeptide–ribosome to the translocon leads to opening of this

translocation channel to admit the growing polypeptide adjacent to the signal sequence, which is transferred to a hydrophobic binding site next to the central pore. Both the SRP and SRP receptor, once dissociated from the translocon, hydrolyze their bound GTP and then are ready to initiate the insertion of another polypeptide chain.

B. As the polypeptide chain elongates, it passes through the translocon channel into the ER lumen, where the signal sequence is cleaved by signal peptidase and is rapidly degraded.

C. The SRP and the nascent polypeptide chain–ribosome complex bind to the SRP receptor in

the ER membrane. This interaction is strengthened by the binding of GTP to both the SRP and its receptor.

D. The ER signal sequence emerges from the ribosome; it is bound by a signal recognition particle (SRP).