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question about NBME 19 - sanam62
#1
what is the answer for this question?
Histone acetyltransferases catalyze the acetylation of lysine residues in the amoni terminal tails of histones. which of the following is the most likely effect of thi covalent modification on chromatin structure?

1. Decreases the affinity of histones for DNA?
2.Increases the affinity of histones for DNA?

Thank you
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#2
Acetylation of lysine side chains in histones destabilizes chromatin structures -> favors transcription.
So, if acetylation eliminates +/charges lysine tail -> What u think gone happen to the binding affinity of histone for the -/charged DNA in HATs path?
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#3
So it cause decrease the binding affinity of histone for the DNA!

Thank you
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