What is ubiquitin ligase? A) The enzyme that transfers ubiquitin onto the 20S subunit from the...
What is ubiquitin ligase?
A) The enzyme that transfers ubiquitin onto the 20S subunit from the protein destined for degradation.
B) The enzyme that removes ubiquitin from proteins in the proteasome.
C) The enzyme that transfers ubiquitin onto proteins that are destined for degradation.
Homework Answers
Answer: (C)
Explanation: Ubiquitination, a post-translational modification of proteins requires the sequential action of three enzymes. E1, or ubiquitin-activating enzyme, catalyzes the ATP-dependent activation of ubiquitin. Ubiquitin is then transferred to a E2 (ubiquitin-conjugating enzymes) and through the E3 (ubiquitin ligase) to the protein substrate destined for degradation by the proteasome.
E3 (ubiquitin ligase) recognize a substrate through specific short amino acid sequences, known as degrons, and catalyze the transfer of ubiquitin from the E2 to the protein substrate.
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What is ubiquitin ligase?
A) The enzyme that transfers ubiquitin onto the 20S subunit from
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to the promoter of a gene so that transcription can be initiated.
The closeup shows the secondary structure of the sigma (?)
subunit, which consists of four domains. Identify the domains
labeled 1-3.
The sigma (?) subunit binds to the core RNA polymerase
enzyme. The function of this sigma factor is to recognize and bind
to...
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A
The sigma (?) subunit binds to the core RNA polymerase
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subunit, which consists of four domains. Identify the domains
labeled 1-3.
The sigma (?) subunit binds to the core RNA polymerase
enzyme. The function of this sigma factor is to recognize and bind
to...
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