Differences in specificity and selectivity between CBP and p300 acetylation of histone H3 and H3/H4.

ABSTRACT: Although p300 and CBP lysine acetyltransferases are often treated interchangeably, the inability of one enzyme to compensate for the loss of the other suggests unique roles for each. As these deficiencies coincide with aberrant levels of histone acetylation, we hypothesized that the key difference between p300 and CBP activity is differences in their specificity/selectivity for lysines within the histones. Utilizing a label-free, quantitative mass spectrometry based technique, we determined the kinetic parameters of both CBP and p300 at each lysine of H3 and H4, under conditions we would expect to encounter in the cell (either limiting acetyl-CoA or histone). Our results show that while p300 and CBP acetylate many common residues on H3 and H4, they do in fact possess very different specifi

SUBMITTER: Henry RA 

PROVIDER: S-EPMC3756530 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature