Protein kinase C coordinates histone H3 phosphorylation and acetylation
- University of Manchester, United Kingdom
- Cited 7
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Abstract
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 reveal an important role for Pkc1 in coordinating the deposition of two different histone modifications that are important for chromatin assembly.
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Reviewing Editor
- Jessica Tyler, University of Texas MD Anderson Cancer Center, United States
Publication history
- Received: July 5, 2015
- Accepted: October 14, 2015
- Accepted Manuscript published: October 15, 2015 (version 1)
- Version of Record published: December 9, 2015 (version 2)
Copyright
© 2015, Darieva et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Further reading
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- Biochemistry and Chemical Biology
- Cell Biology
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- Biochemistry and Chemical Biology
- Structural Biology and Molecular Biophysics
