Conservation and Function of the Histone Methyltransferase Set2 Public Deposited

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  • March 20, 2019
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  • Morris, Stephanie A.
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
Abstract
  • Histone methylation is an important post-translational modification involved in the regulation of eukaryotic gene expression. While many methylation sites on histone proteins have been identified to play roles in both gene activation and repression, the enzymes mediating these modifications and their exact functions are just beginning to be discovered. In the budding yeast Saccharomyces cerevisiae, methylation of histone H3 at lysine 36 (H3K36) by the histone methyltransferase Set2 has been linked to the process of transcription elongation. Previous findings indicate that through an interaction with the elongating RNA polymerase, Set2 targets H3K36 for methylation in the coding region of genes. However, the exact functions for this enzyme and its modification were largely unknown. In these studies, I demonstrate that Set2 methylation of H3K36 is highly conserved and associated with elongating RNA polymerase II in organisms distinct from budding yeast. These results reveal that Set2 and H3K36 methylation have a conserved role in the transcription elongation process. Furthermore, I have contributed to the finding that Set2 regulates global histone acetylation patterns by recruiting a small Rpd3 deacetylase (Rpd3S) complex to the coding region of genes. This is among one of the first studies to identify a functional mechanism for Set2-mediated H3K36 methylation in transcription elongation. Finally, I have identified a novel and conserved modification on H3K36. Independent of being methylated, my studies reveal H3K36 is acetylated by the transcriptional co-activator Gcn5 at promoter regions. Collectively, these results suggest that distinct modifications on H3K36 play diverse roles in the transcription process.
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  • Strahl, Brian
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