Histone-modifying enzymes: encrypting an enigmatic epigenetic code.

Full Abstract

Histone-modifying enzymes catalyze a diverse array of post-translational modifications of core and linker histones within chromatin. These modifications govern a multitude of genomic functions, particularly gene expression, and are believed to constitute an epigenetic code. Histone-modifying enzymes inscribe this code by catalyzing site-selective modifications, which are subsequently interpreted by effector proteins that recognize specific covalent marks. The substrate specificity of these enzymes is of fundamental biological importance because it underpins this epigenetic code. Recently, the structural basis of this specificity has been examined with regards to recently determined structures of GCN5 acetyltransferases and SET domain methyltransferases in complex with their cognate histone substrates.

Learn Faster Today Improve your study skills

Author information

Author/s: Couture, Jean-François (JF); Trievel, Raymond C (RC);

Affiliation: Department of Biological Chemistry, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, MI 48109-0606, USA.

Grants: GM073839 (Agency:NIGMS NIH HHS)

Journal and publication information

Publication Type: In Vitro; Journal Article; Research Support, N.I.H., Extramural; Review

Journal: Current opinion in structural biology (Curr Opin Struct Biol), published in England. (Language: eng)

Reference: 2006-Dec; vol 16 (issue 6) : pp 753-60

Dates: Created 2006/12/04; Completed 2007/01/31; Revised 2007/12/03;

PMID: 17070031, status: MEDLINE (last retrieval date: 12/26/2008)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

External Links for this article (including full text providers, if available):

Click Electronic Full-text Provider Links to see options for finding the electronic full text links to this article. Note there may be a subscription or fee required for access to the full text. See our FAQ for information on finding FREE full text articles.

This article may also be located in paper journal collections available in many libraries. Use the Journal and Publication Information above to find the full article.

MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals
Catalytic Domain
Epigenesis, Genetic
Histone Acetyltransferases - chemistry; metabolism
Histone-Lysine N-Methyltransferase - chemistry; metabolism
Histones - metabolism
Humans

Humans
Models, Molecular
Protein Conformation
Protein Processing, Post-Translational
Saccharomyces cerevisiae Proteins - chemistry; metabolism
Substrate Specificity
Tetrahymena thermophila - enzymology

Associated Chemicals: Histones (0) ; Saccharomyces cerevisiae Proteins (0) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; Esa1 protein, S cerevisiae (EC 2.3.1.48) ; Histone Acetyltransferases (EC 2.3.1.48) ; tGCN5 histone acetyltransferase (EC 2.3.1.48)

These are the highest related articles currently in the database:

See 100+ related articles.