Ontology highlight
ABSTRACT:
SUBMITTER: Park YJ
PROVIDER: S-EPMC2680711 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Park Young-Jun YJ Sudhoff Keely B KB Andrews Andrew J AJ Stargell Laurie A LA Luger Karolin K
Nature structural & molecular biology 20080901 9
Rtt109 is a histone acetyltransferase that requires a histone chaperone for the acetylation of histone 3 at lysine 56 (H3K56). Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. Here we show that both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis. The C-terminal acidic domain of Vps75 contributes to activation of Rtt109 and is necessary for in vivo functionality of Vps75, but it is not requ ...[more]