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Mol Cell. 2005 Apr 1;18(1):123-30.

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

Author information

1
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.

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.

PMID:
15808514
PMCID:
PMC2855496
DOI:
10.1016/j.molcel.2005.02.031
[Indexed for MEDLINE]
Free PMC Article

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