Ontology highlight
ABSTRACT:
SUBMITTER: Ye J
PROVIDER: S-EPMC2855496 | biostudies-literature | 2005 Apr
REPOSITORIES: biostudies-literature
Ye Jianxin J Ai Xi X Eugeni Ericka E EE Zhang Liwen L Carpenter Laura Rocco LR Jelinek Mary A MA Freitas Michael A MA Parthun Mark R MR
Molecular cell 20050401 1
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 su ...[more]