Ontology highlight
ABSTRACT:
SUBMITTER: Albaugh BN
PROVIDER: S-EPMC3137045 | biostudies-literature | 2011 Jul
REPOSITORIES: biostudies-literature
Albaugh Brittany N BN Arnold Kevin M KM Lee Susan S Denu John M JM
The Journal of biological chemistry 20110523 28
Rtt109 is a yeast histone acetyltransferase (HAT) that associates with histone chaperones Asf1 and Vps75 to acetylate H3K56, H3K9, and H3K27 and is important in DNA replication and maintaining genomic integrity. Recently, mass spectrometry and structural studies of Rtt109 have shown that active site residue Lys-290 is acetylated. However, the functional role of this modification and how the acetyl group is added to Lys-290 was unclear. Here, we examined the mechanism of Lys-290 acetylation and f ...[more]