#Question id: 4541
#Unit 3. Fundamental Processes
Mig1 recruits a “repressing complex” containing the Tup1 protein. This complex is recruited by many yeast DNA-binding proteins that repress transcription, including the alpha2 protein involved in controlling the mating-type specific. Tup1 also has counterparts in mammalian cells, choose correct mechanisms have been proposed to explain the repressing effect of Tup1.
I-Tup1 acts on nucleosomes either through recruiting histone deacetylases and/or by positioning a nucleosome at or near the transcription start site.
II-Tup1 interacts directly with the transcriptional machinery at the promoter and inhibits initiation.
#Question id: 4542
#Unit 3. Fundamental Processes
Repression of the GAL1 gene in yeast by Mig1, in the presence of glucose follows those steps;
I- Deacetylation of local nucleosomes
II-Recruiting the Tup1 repressing complex
III- Mig1 represses expression of GAL1
IV- Mig1 binds a site between the UASG and the GAL1 promoter
#Question id: 4543
#Unit 3. Fundamental Processes
Control of the activator NtrC- In that case, the signal (low ammonia levels) induces a kinase that phosphorylates NtrC. This is type of
A. Indirect signaling
B. Direct signaling
C. Is an example of a signal transduction pathway
#Question id: 4544
#Unit 3. Fundamental Processes
How is the binding of ligand to the extracellular domain communicated to the intracellular domain?
#Question id: 4545
#Unit 3. Fundamental Processes
Through which signal transduction pathway- controls the activators such as Jun, one of the activators that works at the interferon-beta enhancer
#Question id: 4546
#Unit 3. Fundamental Processes
In eukaryotes, transcriptional regulators are not typically controlled at the level of DNA binding (although there are exceptions). Regulators are instead usually controlled in one of the following two basic ways.
I. Unmasking an Activating Region
II. Transport into and out of the Nucleus
III. Mediated through proteolysis of an inhibitor or tethering region or by allosteric changes.
IV. Also is itself (or recruits) a deacetylase,