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- W2017754734 abstract "The histone acetyltransferase (HAT) p300/CBP has been shown to undergo autoacetylation on lysines in an apparent regulatory loop that stimulates HAT activity. Here we have developed a strategy to introduce acetyl-Lys at up to six known modification sites in p300/CBP HAT using a combination of circular permutation and expressed protein ligation. We show that these semisynthetic, circularly permuted acetylated proteins retain high affinity for an acetyl-CoA substrate analogue and that HAT activity correlates positively with degree of acetylation. This study provides novel evidence for control of p300/CBP HAT activity by site-specific autoacetylation and outlines a potentially general strategy for using expressed protein ligation and circular permutation to chemically interrogate internal regions of proteins." @default.
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- W2017754734 date "2010-02-03" @default.
- W2017754734 modified "2023-10-16" @default.
- W2017754734 title "Analysis of p300/CBP Histone Acetyltransferase Regulation Using Circular Permutation and Semisynthesis" @default.
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- W2017754734 doi "https://doi.org/10.1021/ja909466d" @default.
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