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9 Jan 2018

What is the 26S proteasome? What are the respective roles of the 19S and 20S proteasomes in protein degradation

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Irving Heathcote
Irving HeathcoteLv2
11 Jan 2018
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Related questions

1. Not only are amino acids required for the synthesis of proteins, but some amino acids (particularly the branched chain amino acid leucine) can function as signaling molecules. Of particular importance to nutrition is a protein complex known as mammalian target of rapamycin (mTORC1) that is activated in response to leucine. Using your advanced research skills, discuss the mechanisms through which leucine signals an increase in protein synthesis through the activation of mTORC1. You may find it useful to focus on ribosomal protein S6 kinase (S6K1) and eukaryotic initiation factor 4E binding protein (eIF4E-BP).

2. Amino acid deprivation leads to the inhibition of mTOR signaling and stimulates protein degradation through autophagy (lysosomal proteolysis). In addition to autophagy, amino acid deprivation also activates the ubiquitin proteasome system. Ubiquitin (Ub) is a small peptide that is attached to some proteins so that they are directed to the proteasome. Illustrate the role(s) of Ub-activating enzyme (E1), Ub-conjugating enzymes (E2), and Ub-ligases (E3) as they relate to protein ubiquitylation.

3. Explain the role of the 26S proteasome as it relates to proteasomal degradation. Also discuss requirements, if any, for energy in this process.

(A) Which stand of the miRNA duplex is incorporated into the miRISC complex? Select one:

a. guide strand b. passenger strand c. sense strand d. none of these answers e. antisense DNA strand

(B) Generally speaking, the class of proteins that conjugate ubiquitin to target proteins are referred to as the ___________. Select one:

a. 20S core b. E2 ligases c. E1 ligases d. E3 ligases e. 19S regulatory particle

(C) E3 ubiquitin ligases require 2 specific domains that interact with the ______ and _____. Select one:

a. none of these b. target and proteasome lid c. E1 and E2 proteins d. target and E1 proteins e. target and E2 proteins

What are codons, the genetic code, redundancy, and reading frames?

What are the important structural features of a tRNA?

What is the relationship between the number of possible codons, amino acids, and tRNAs?

What is tRNA charging? What is the enzyme responsible for tRNA charging?

What are ribosomes made of? What are the roles of the large and small subunit? What are the E, P, and A sites? What is the function of the rRNAs?

What are the steps in translation including initiation, elongation, and termination? What are the roles of the initiator tRNA, translation initiation factors, EF-Tu/EF1, EF-G/EF2, and release factors?

What is the match between a codon and tRNA proofread?

What is a polysome?

What do proteasomes, ubiquitin, and proteases have to do with protein degradation (proteolysis)?

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