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PMID: 15184976 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Structures of protein domains that create or recognize histone modifications.

EMBO reports ·Vol. 5 ·No. 5 ·2004-05-00 ·Pages 464-9

Bottomley MJ

Abstract

DNA is packed together with histone proteins in cell nuclei to form a compact structure called chromatin. Chromatin represents a scaffold for many genetic events and shows varying degrees of condensation, including a relatively open form (euchromatin) and a highly condensed form (heterochromatin). Enzymes such as histone acetyltransferases (HATs) and methylases covalently label the amino-termini of histones, thereby creating a 'histone code' of modifications that is interpreted by the recruitment of other proteins through recognition domains. Ultimately, this network of interacting proteins is thought to control the degree of chromatin condensation so that DNA is available when it is required for genomic processes. Reviewed here are the structures of HAT and SET domains, which mediate the acetylation and methylation of histones, respectively, and bromodomains and chromodomains, which recognize the modified histones. How these structures have increased our understanding of DNA regulation is also discussed.

MeSH Terms
Acetylation Acetyltransferases/chemistry,metabolism Amino Acid Sequence Chromatin/chemistry,metabolism Gene Expression Regulation Histone Acetyltransferases Histones/chemistry,metabolism Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Phosphorylation Protein Conformation
Chemicals
Chromatin Histones Acetyltransferases Histone Acetyltransferases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Bottomley Matthew J
Istituto di Ricerche di Biologia Molecolare, Via Pontina Km 30.600, 00040 Pomezia (Rome), Italy. [email protected]
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Article Info
Journal
EMBO reports
Abbr.
EMBO Rep
ISSN
1469-221X
DOI
10.1038/sj.embor.7400146
Email
[email protected]
Published
2004-05-00
Pages
464-9
Language
English
Region
England
NLM ID
100963049
PMCID
PMC1299057
Subset
IM
External Links
PubMed source DOI: 10.1038/sj.embor.7400146 PMC Full Text View journal details
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