Histone H3 serine 57 and lysine 56 interplay in transcription elongation and recovery from S-phase stress.

ABSTRACT:

Background

Acetylation of lysine 56 of histone H3 plays an important role in the DNA damage response and it has been postulated to play an as yet undefined role in transcription, both in yeast and in higher eukaryotes. Because phosphorylated human histone H3 serine 57 peptides have been detected by mass spectrometry we examined whether H3-S57 phosphorylation interplays with H3-K56 acetylation in vivo.

Methodology/principal findings

To explore the physiological role of H3-S57, H3-K56 was mutated to mimic constitutively (un)acetylated forms of H3-K56 and these were combined with constitutively (un)phosphorylated mimics of H3-S57, in yeast. A phosphorylated serine mimic at position 57 lessened sensitivities to a DNA replication fork inhibitor and to a transcription elongation i

SUBMITTER: Aslam A 

PROVIDER: S-EPMC2877106 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature