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PMID: 10839822 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Acetylation of histones and transcription-related factors.

Microbiology and molecular biology reviews : MMBR ·Vol. 64 ·No. 2 ·2000-06-00 ·Pages 435-59

Sterner DE, Berger SL

Abstract

The state of chromatin (the packaging of DNA in eukaryotes) has long been recognized to have major effects on levels of gene expression, and numerous chromatin-altering strategies-including ATP-dependent remodeling and histone modification-are employed in the cell to bring about transcriptional regulation. Of these, histone acetylation is one of the best characterized, as recent years have seen the identification and further study of many histone acetyltransferase (HAT) proteins and their associated complexes. Interestingly, most of these proteins were previously shown to have coactivator or other transcription-related functions. Confirmed and putative HAT proteins have been identified from various organisms from yeast to humans, and they include Gcn5-related N-acetyltransferase (GNAT) superfamily members Gcn5, PCAF, Elp3, Hpa2, and Hat1: MYST proteins Sas2, Sas3, Esa1, MOF, Tip60, MOZ, MORF, and HBO1; global coactivators p300 and CREB-binding protein; nuclear receptor coactivators SRC-1, ACTR, and TIF2; TATA-binding protein-associated factor TAF(II)250 and its homologs; and subunits of RNA polymerase III general factor TFIIIC. The acetylation and transcriptional functions of these HATs and the native complexes containing them (such as yeast SAGA, NuA4, and possibly analogous human complexes) are discussed. In addition, some of these HATs are also known to modify certain nonhistone transcription-related proteins, including high-mobility-group chromatin proteins, activators such as p53, coactivators, and general factors. Thus, we also detail these known factor acetyltransferase (FAT) substrates and the demonstrated or potential roles of their acetylation in transcriptional processes.

MeSH Terms
Acetylation Acetyltransferases/chemistry,physiology Animals Gene Products, tat/metabolism High Mobility Group Proteins/metabolism Histone Acetyltransferases Histones/metabolism Humans Nucleosomes/metabolism Saccharomyces cerevisiae Proteins Transcription Factors/metabolism
Chemicals
Gene Products, tat High Mobility Group Proteins Histones Nucleosomes Saccharomyces cerevisiae Proteins Transcription Factors Acetyltransferases Histone Acetyltransferases KAT7 protein, human KAT8 protein, human
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sterner D E
The Wistar Institute, Philadelphia, Pennsylvania 19104, USA.
Berger S L
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Article Info
Journal
Microbiology and molecular biology reviews : MMBR
Abbr.
Microbiol Mol Biol Rev
ISSN
1092-2172
DOI
10.1128/MMBR.64.2.435-459.2000
Published
2000-06-00
Pages
435-59
Language
English
Region
United States
NLM ID
9706653
PMCID
PMC98999
Subset
IM
External Links
PubMed source DOI: 10.1128/MMBR.64.2.435-459.2000 PMC Full Text View journal details
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