Histone acetyltransferases: function, structure, and catalysis (Q28204852)

Current Opinion in Genetics & Development

Europe PubMed Central

title

Histone acetyltransferases: function, structure, and catalysis (English)

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author name string

R Marmorstein

series ordinal

1

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S Y Roth

series ordinal

2

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language of work or name

English

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publication date

April 2001

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published in

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volume

11

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issue

2

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page(s)

155-61

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cites work

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Acetylation of histones and transcription-related factors

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Roles of histone acetyltransferases and deacetylases in gene regulation

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ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation

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The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

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A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme

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The language of covalent histone modifications

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Acetylation: a regulatory modification to rival phosphorylation?

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Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

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Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo

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Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo

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Structure and ligand of a histone acetyltransferase bromodomain

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Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases

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Esa1p is an essential histone acetyltransferase required for cell cycle progression

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The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein

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Chromodomains are protein-RNA interaction modules

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Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

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Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A

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Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases

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Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator

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Mutations truncating the EP300 acetylase in human cancers

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Histone acetylases and deacetylases in cell proliferation

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

2408850

2408850

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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