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Chromatin condensation is facilitated by SMC proteins which act

Chromatin condensation is facilitated by SMC proteins which act

Question
46. Chromatin condensation is facilitated by SMC proteins which act to:

A. Disassemble histone proteins

B. Act as a scaffold to support highly condensed DNA

C. Interfere with negatively charged phosphate backbones

D. Daisy-chain nucleosomes

E. Block the formation of the 30nm fibre

47. SWI/SNF complexes contain up to 1 1 different subunits, one of which contains a motif important for acetylation recognition called a:

A. Bromodomain

B. Chromodomain

C. Ligand binding domain

D. RNA polymerase activity.

E. Helicase

48. The vitamin D receptor (VDR) binds to and activates the Cyp24 promoter. You obtain a plasmid that contains the Cyp24 promoter upstream of the lacZ reporter gene. From this you create two new plasmids that each contain a different mutation in the Cyp24 promoter: mutation A and mutation B, each of which may be VDR binding elements. When you transfect each plasmid into cells, you observe that the plasmid containing mutation A results in 2-fold less ßgalactosidase activity compared to the unmutated plasmid. You also observe that the plasmid containing mutation B results in equivalent ß-galactosidase activity compared to the unmutated plasmid. What can you conclude from this experiment?

A. Mutation A completely abolishes VDR binding.

B. Both mutation A and B completely abolish VDR binding.

C. Mutation B is in a VDR binding site, but mutation A is not.

D. Mutation A is in a VDR binding site, but mutation B is not.

E. VDR binding to the Cyp24 promoter actually suppresses promoter activity

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49. Which of the following is true of histone tails?

A. They protrude between the two DNA strands that supercoil around the nucleosome.

B. They are the target of numerous chemical modifications.

C. They experience changes in net charge, shape, and other properties of histones in response to modifications.

D. They are recognized by acetylases and methylases.

E. All of the above

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