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PMID: 15808514 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.

Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly.

Molecular cell ·Vol. 18 ·No. 1 ·2005-04-01 ·Pages 123-30

Ye J, Ai X, Eugeni EE, Zhang L, Carpenter LR, Jelinek MA, Freitas MA, Parthun MR

Abstract

The acetylation of the NH2-terminal tail of histone H4 by type B histone acetyltransferases (HATs) is involved in the process of chromatin assembly. Histone H4 associated with a nuclear type B HAT complex contains modifications in its globular core domain as well. In particular, acetylation was found at lysine 91. A mutation that alters this residue, which lies in the interface between histone H3/H4 tetramers and H2A/H2B dimers, confers phenotypes consistent with defects in chromatin assembly such as sensitivity to DNA damaging agents and derepression and alteration of silent chromatin structure. In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structure. These results indicate an important role for histone modifications outside the NH2-tail domains in the processes of chromatin assembly, DNA repair, and transcriptional silencing.

MeSH Terms
Acetylation Cell Nucleus/metabolism Chromatin/metabolism Dimerization Histones/chemistry,genetics,metabolism Lysine/metabolism Protein Isoforms/chemistry,genetics,metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins/chemistry,genetics,metabolism
Chemicals
Chromatin Histones Protein Isoforms Saccharomyces cerevisiae Proteins Lysine
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Ye Jianxin
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Ai Xi
Eugeni Ericka E
Zhang Liwen
Carpenter Laura Rocco
Jelinek Mary A
Freitas Michael A
Parthun Mark R
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Article Info
Journal
Molecular cell
Abbr.
Mol Cell
ISSN
1097-2765
DOI
10.1016/j.molcel.2005.02.031
Published
2005-04-01
Pages
123-30
Language
English
Region
United States
NLM ID
9802571
PMCID
PMC2855496
Subset
IM
Grants
NIGMS NIH HHS · R01 GM062970 · United States
NIGMS NIH HHS · R01 GM62970 · United States
NCI NIH HHS · R01 CA107106-01 · United States
NCI NIH HHS · R01 CA107106-04 · United States
NCI NIH HHS · R01 CA107106-03 · United States
NCI NIH HHS · R01 CA107106 · United States
NCI NIH HHS · R01 CA107106-02 · United States
External Links
PubMed source DOI: 10.1016/j.molcel.2005.02.031 PMC Full Text View journal details
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