Protein kinase C coordinates histone H3 phosphorylation and acetylation

eLife

Zoulfia Darieva¹  Andrew D Sharrocks¹  Aaron Webber¹  Stacey Warwood¹ 

[1] Faculty of Life Sciences, University of Manchester, Manchester, United Kingdom;

关键词: protein kinase C;    histone;    acetylation;    Rtt109;    phosphorylation;   

DOI  :  10.7554/eLife.09886

来源: DOAJ

【 摘 要 】

The re-assembly of chromatin following DNA replication is a critical event in the maintenance of genome integrity. Histone H3 acetylation at K56 and phosphorylation at T45 are two important chromatin modifications that accompany chromatin assembly. Here we have identified the protein kinase Pkc1 as a key regulator that coordinates the deposition of these modifications in S. cerevisiae under conditions of replicative stress. Pkc1 phosphorylates the histone acetyl transferase Rtt109 and promotes its ability to acetylate H3K56. Our data also reveal novel cross-talk between two different histone modifications as Pkc1 also enhances H3T45 phosphorylation and this modification is required for H3K56 acetylation. Our data therefore uncover an important role for Pkc1 in coordinating the deposition of two different histone modifications that are important for chromatin assembly.

【 授权许可】

Unknown