Dataset Information

Quantitative Histone Acetylation

ABSTRACT: This work details a previously uncharacterized cross-talk between the Gcn5 bromodomain "reader" function and enzymatic HAT activity that may ultimately affect gene expression.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Haploid Cell

SUBMITTER: Alan Tackett

LAB HEAD: Alan J Tackett

PROVIDER: PXD001167 | Pride | 2014-08-14

REPOSITORIES: Pride

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Publications

The bromodomain of Gcn5 regulates site specificity of lysine acetylation on histone H3.

Cieniewicz Anne M AM Moreland Linley L Ringel Alison E AE Mackintosh Samuel G SG Raman Ana A Gilbert Tonya M TM Wolberger Cynthia C Tackett Alan J AJ Taverna Sean D SD

Molecular & cellular proteomics : MCP 20140808 11

In yeast, the conserved histone acetyltransferase (HAT) Gcn5 associates with Ada2 and Ada3 to form the catalytic module of the ADA and SAGA transcriptional coactivator complexes. Gcn5 also contains an acetyl-lysine binding bromodomain that has been implicated in regulating nucleosomal acetylation in vitro, as well as at gene promoters in cells. However, the contribution of the Gcn5 bromodomain in regulating site specificity of HAT activity remains unclear. Here, we used a combined acid-urea gel ...[more]

PMID: 25106422

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			Action	DRS
	F002483.dat	Other
	F002483.dat-pride.pride.mgf.gz	Mgf
	F002483.dat-pride.pride.mztab.gz	Mztab
	F002483.dat-pride.xml.gz	Xml
	F002484.dat	Other