Abstract
Histone acetylation has been shown to be required for the proper regulation of many cellular processes including transcription, DNA repair, and chromatin assembly. Acetylation of histone H3 on lysine 56 (H3K56) occurs both during the premeiotic and mitotic S phase and persists throughout DNA damage repair. To learn more about the molecular mechanism of H3K56 acetylation and factors required for this process, we surveyed the genome of the yeast Saccharomyces cerevisiae to identify genes necessary for this process. A comparative global proteomic screen identified several factors required for global H3K56 acetylation, which included histone chaperone Asf1 and a protein of an unknown function Rtt109 but not Spt10. Our results indicate that the loss of Rtt109 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin, similar to that of asf1Delta or the K56Q mutation. RTT109 deletion exhibits sensitivity to DNA damaging agents similar to that of asf1Delta and H3K56Q mutants. Furthermore, Rtt109 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of polymerase II in yeast. This histone modification is also associated with some of the transcriptionally active puff sites in Drosophila. Our results indicate a new role for the Rtt109 protein in the proper regulation of H3K56 acetylation.
Highlights
Histone acetylation has been shown to be required for the proper regulation of many cellular processes including transcription, DNA repair, and chromatin assembly
Employing global proteomic screen (GPS), we have demonstrated that several factors including the histone chaperone protein, Asf1 as well as a protein of unknown function, Rtt109, are required for global H3K56 acetylation both from bulk histone and on chromatin
It was demonstrated via chromatin immunoprecipitation (ChIP) studies that Spt10 is required for proper cell cycle-specific H3K56 acetylation at histone genes [10], our data indicate that this putative histone acetyltransferase is dispensable for global acetylation of H3K56
Summary
Rtt109 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of polymerase II in yeast. Employing GPS, we have demonstrated that several factors including the histone chaperone protein, Asf as well as a protein of unknown function, Rtt109, are required for global H3K56 acetylation both from bulk histone and on chromatin. It was demonstrated via chromatin immunoprecipitation (ChIP) studies that Spt is required for proper cell cycle-specific H3K56 acetylation at histone genes [10], our data indicate that this putative histone acetyltransferase is dispensable for global acetylation of H3K56. We show that the association of H3K56 acetylation as a
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