Histone H3 Thr 45 phosphorylation is a replication-associated post-translational modification in S. cerevisiae.

ABSTRACT: Post-translational histone modifications are crucial for the regulation of numerous DNA-templated processes, and are thought to mediate both alteration of chromatin dynamics and recruitment of effector proteins to specific regions of the genome. In particular, histone Ser/Thr phosphorylation regulates multiple nuclear functions in the budding yeast Saccharomyces cerevisiae, including transcription, DNA damage repair, mitosis, apoptosis and sporulation. Although modifications to chromatin during replication remain poorly understood, a number of recent studies have described acetylation of the histone H3 N-terminal alpha-helix (alphaN helix) at Lys 56 as a modification that is important for maintenance of genomic integrity during DNA replication and repair. Here, we report phosphorylation of

SUBMITTER: Baker SP 

PROVIDER: S-EPMC2856316 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature