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PMID: 16263263 Published · ppublish English Journal Article Review

Structure and activity of enzymes that remove histone modifications.

Current opinion in structural biology ·Vol. 15 ·No. 6 ·2005-12-00 ·Pages 673-80

Holbert MA, Marmorstein R

Abstract

The post-translational modification of histones plays an important role in chromatin regulation, a process that insures the fidelity of gene expression and other DNA transactions. Equally important as the enzymes that generate these modifications are the enzymes that remove them. Recent studies have identified some of the enzymes that remove histone modifications and have characterized their activities. In addition, structural and biochemical studies of these enzymes have focused on the histone lysine deacetylases HDAC8 and sirtuins, and on the arginine and lysine demethylases PAD and BHC110/LSD1, respectively. These new findings may be used as a context to present new information that contributes to our understanding of chromatin regulation, and to pose remaining questions pertaining to the activities of these enzymes and the roles they play in chromatin regulation.

MeSH Terms
Animals Histone Deacetylases/chemistry,metabolism Histone Demethylases Histones/metabolism Humans Methylation Models, Molecular Oxidoreductases, N-Demethylating/chemistry,metabolism Protein Conformation Protein Processing, Post-Translational Repressor Proteins/chemistry,metabolism Sirtuins/chemistry,metabolism
Chemicals
Histones Repressor Proteins Histone Demethylases KDM1A protein, human Oxidoreductases, N-Demethylating Sirtuins HDAC8 protein, human Histone Deacetylases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Holbert Marc A
The Wistar Institute and The Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
Marmorstein Ronen
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2005-12-00
Epub
2005-00-02
Pages
673-80
Language
English
Region
England
NLM ID
9107784
Subset
IM
Grants
NIGMS NIH HHS · R01 GM060293 · United States
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