Ontology highlight
ABSTRACT:
SUBMITTER: Lercher L
PROVIDER: S-EPMC5861439 | biostudies-literature | 2018 Mar
REPOSITORIES: biostudies-literature
Lercher Lukas L Danilenko Nataliya N Kirkpatrick John J Carlomagno Teresa T
Nucleic acids research 20180301 5
Acetylation of histone H3 at lysine-56 by the histone acetyltransferase Rtt109 in lower eukaryotes is important for maintaining genomic integrity and is required for C. albicans pathogenicity. Rtt109 is activated by association with two different histone chaperones, Vps75 and Asf1, through an unknown mechanism. Here, we reveal that the Rtt109 C-terminus interacts directly with Asf1 and elucidate the structural basis of this interaction. In addition, we find that the H3 N-terminus can interact vi ...[more]