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PMID: 17306844 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Mechanisms of ATP dependent chromatin remodeling.

Mutation research ·Vol. 618 ·No. 1-2 ·2007-05-01 ·Pages 3-17

Gangaraju VK, Bartholomew B

Abstract

The inter-relationship between DNA repair and ATP dependent chromatin remodeling has begun to become very apparent with recent discoveries. ATP dependent remodeling complexes mobilize nucleosomes along DNA, promote the exchange of histones, or completely displace nucleosomes from DNA. These remodeling complexes are often categorized based on the domain organization of their catalytic subunit. The biochemical properties and structural information of several of these remodeling complexes are reviewed. The different models for how these complexes are able to mobilize nucleosomes and alter nucleosome structure are presented incorporating several recent findings. Finally the role of histone tails and their respective modifications in ATP-dependent remodeling are discussed.

MeSH Terms
Adenosine Triphosphate/chemistry Animals Catalytic Domain Chromatin/chemistry,genetics,metabolism Chromatin Assembly and Disassembly Diffusion Histones/chemistry Humans Nucleosomes/chemistry,metabolism Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae/metabolism
Chemicals
Chromatin Histones Nucleosomes Adenosine Triphosphate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gangaraju Vamsi K
Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL. 62901-4413, USA.
Bartholomew Blaine
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Article Info
Journal
Mutation research
Abbr.
Mutat Res
ISSN
0027-5107
DOI
10.1016/j.mrfmmm.2006.08.015
Published
2007-05-01
Epub
2007-00-21
Pages
3-17
Language
English
Region
Netherlands
NLM ID
0400763
PMCID
PMC2584342
Subset
IM
Grants
NIGMS NIH HHS · R01 GM048413 · United States
NIGMS NIH HHS · R01 GM070864 · United States
NIGMS NIH HHS · GM48413 · United States
NIGMS NIH HHS · GM70864 · United States
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PubMed source DOI: 10.1016/j.mrfmmm.2006.08.015 PMC Full Text View journal details
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