Question

1. What keeps TFIIF from stimulating a specific phosphatase to remove the phosphate groups from the CTD while RNA pol II is still in the preinitiation complex (PIC)?
   1. Contact with mediator through SRB4
   2. Contact with TFIIB
   3. Contact with TFIIA through the large subunit (TFIIA alpha)
   4. Cdk8 of mediator represses TFIIF activity

2. Which of the following would most likely NOT be found in the promoter of a typical housekeeping (constitutive) gene?
   1. TATAA
   2. Initiator region
   3. Enhancer element
   4. CpG island

3. How is the mediator thought to regulate the rate of initiation and reinitiation?
   1. The tail module makes direct contacts with RNA polymerase II
   2. It provides a helicase to assist in the melting of the promoter
   3. Its conformation controls the rate of entry of RNA pol II in to the preinitiator complex (PIC) it also facilitates the opening of the clamp to allow DNA access to the active site
   4. The CAK module phosphorylates RAP74
   5. Through mono-ubiquitination of histone H1

4. Which of the following complexes is responsible for directly positioning RNA pol III at the start of transcription?
   1. TFIIIC
   2. TFIIIA
   3. TFIIIB
   4. SL1
5. What is the function of the N-terminal domain of TAF1?
   1. It contains a zinc ribbon domain used to bind RAP30
   2. It mimics the structure of the TATAA element and binds to the concave surface of TBP thereby inhibiting the binding of TFIID to the promoter
   3. It positions histone H1 for phosphorylation by the bipartite kinase domain
   4. It contains a fused ubiquitin domain that seems to be involved in the degradation of TFIID during programmed death cell

Answer 1

1) The correct answer is option B) contact with TFIIB.

2) The correct answer is option B) Initiator region

3)The correct answer is option A) The tail module makes direct contact with RNA polymerase II

4)The correct answer is option A) TFIIIC

5) The correct answer is option B) It mimics the structure of the TATAA element and binds to the concave surface of TBP thereby inhibiting the binding of TFIID to the promoter.