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Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE162459 | GEO | 2021/01/01

REPOSITORIES: GEO

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Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [ChIP-seq]

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Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [RNA-seq]

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Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation

Project description:Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation

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Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [ChIP-seq]

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Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [RNA-seq]

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Analysis of p300/CBP histone acetyltransferase regulation using circular permutation and semisynthesis.

Project description: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.

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Project description:Recent studies indicate that histones are subjected to various types of acylation including acetylation, propionylation and crotonylation. CBP and p300 have been shown to catalyze multiple types of acylation but are not conserved in evolution, raising the question as to the existence of other enzymes for histone acylation and the functional relationship between well-characterized acetylation and other types of acylation. In this study, we focus on enzymes catalyzing histone crotonylation and demonstrate that among the known histone acetyltransferases, MOF, in addition to CBP and p300, also possesses histone crotonyltransferase (HCT) activity and this activity is conserved in evolution. We provide evidence that CBP and p300 are the major HCTs in mammalian cells. Furthermore, we have generated novel CBP/p300 mutants with deficient histone acetyltransferase but competent HCT activity. These CBP/p300 mutants can substitute the endogenous CBP/p300 to enhance transcriptional activation in the cell, which correlates with enhanced promoter crotonylation and recruitment of DPF2, a selective reader for crotonylated histones. Taken together, we have identified MOF as an evolutionarily conserved HCT and provide first cellular evidence that CBP/p300 can facilitate transcriptional activation through histone acylation other than acetylation, thus supporting an emerging role for the non-acetylation type of histone acylation in transcription and possibly other chromatin-based processes.

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