Open AccessMethylation of Histone H3 Mediates the Association of the NuA3 Histone Acetyltransferase with Chromatin
Author(s) -
David G. Martin,
Daniel E. Grimes,
Kristin Baetz,
LeAnn Howe
Publication year - 2006
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.26.8.3018-3028.2006
Subject(s) - histone methyltransferase , biology , histone methylation , histone h2a , histone code , histone h3 , histone h1 , ezh2 , histone octamer , nucleosome , chromatin , histone , histone acetyltransferase , microbiology and biotechnology , genetics , dna methylation , dna , gene expression , gene
TheSAS3 -dependent NuA3 histone acetyltransferase complex was originally identified on the basis of its ability to acetylate histone H3 in vitro. Whether NuA3 is capable of acetylating histones in vivo, or how the complex is targeted to the nucleosomes that it modifies, was unknown. To address this question, we asked whether NuA3 is associated with chromatin in vivo and how this association is regulated. With a chromatin pulldown assay, we found that NuA3 interacts with the histone H3 amino-terminal tail, and loss of the H3 tail recapitulates phenotypes associated with loss ofSAS3 . Moreover, mutation of histone H3 lysine 14, the preferred site of acetylation by NuA3 in vitro, phenocopies a uniquesas3 Δ phenotype, suggesting that modification of this residue is important for NuA3 function. The interaction of NuA3 with chromatin is dependent on the Set1p and Set2p histone methyltransferases, as well as their substrates, histone H3 lysines 4 and 36, respectively. These results confirm that NuA3 is functioning as a histone acetyltransferase in vivo and that histone H3 methylation provides a mark for the recruitment of NuA3 to nucleosomes.