Abstract
Modification of histone amino terminal tails by acetylation has long been linked to the transcriptional capacity of genes in chromatin and to various aspects of chromatin dynamics. Over the last few years a flurry of reports have described the purification and identification of a large number of histone acetyltransferases. Many of these enzymes had previously been described as transcriptional regulators and have frequently been isolated as part of larger multisubunit protein complexes. This review describes the association of acetyltransferases with partner proteins and the additional functional attributes of such complexes beyond catalytic function.
Copyright 1999 Academic Press.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Review
MeSH terms
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Acetylation
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Acetyltransferases / metabolism*
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Animals
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CREB-Binding Protein
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Chromatin / metabolism
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Fungal Proteins / metabolism
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Gene Expression Regulation / physiology
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Histone Acetyltransferases
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Histones / chemistry
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Histones / metabolism*
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Humans
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Macromolecular Substances
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Multigene Family
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Nuclear Proteins / metabolism
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Nucleosomes / metabolism
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Protein Processing, Post-Translational*
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Protozoan Proteins / metabolism
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins*
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Signal Transduction / physiology*
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Tetrahymena thermophila / metabolism
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Trans-Activators / metabolism
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Transcription Factor TFIID
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Transcription Factors / metabolism
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Transcription Factors, TFII / metabolism
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Transcription, Genetic
Substances
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Chromatin
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Fungal Proteins
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Histones
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Macromolecular Substances
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Nuclear Proteins
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Nucleosomes
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Protozoan Proteins
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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Transcription Factor TFIID
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Transcription Factors
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Transcription Factors, TFII
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Acetyltransferases
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CREB-Binding Protein
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CREBBP protein, human
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Histone Acetyltransferases