Unravelling the role of Set2 protein domains in H3K36 methylation in Saccharomyces cerevisiae

Authors

  • Saima Nazir Department of Biochemistry; University of Kashmir
  • Urseela Yasien Centre for Interdisciplinary Research and Innovations (CIRI); University of Kashmir
  • Aaqib Ashraf Department of Clinical Biochemistry; University of Kashmir
  • Showkat Ahmad Ganie Department of Clinical Biochemistry; University of Kashmir
  • Abdul Wajid Bhat Centre for Interdisciplinary Research and Innovations (CIRI); Department of Clinical Biochemistry, University of Kashmir,

DOI:

https://doi.org/10.22364/eeb.22.09

Keywords:

halophyte, ion accumulation, Mertensia maritima, mineral nutrition, propagation, salinity, temporary immersion system, tissue culture

Abstract

Histone methylation plays a crucial role in gene expression and chromatin structure regulation. In Saccharomyces cerevisiae, the Set2 protein is responsible for the methylation of histone H3 at lysine 36 (H3K36), which is associated with transcriptional regulation, RNA processing, and DNA repair. This study investigates the specific functions of individual domains within the yeast Set2 protein by utilizing PCR-based domain deletions and subsequent western blot analysis to assess their impact on H3K36 methylation status. The results demonstrate that the SET domain alone is sufficient for H3K36 dimethylation, while optimal trimethylation necessitates the presence of additional domains, including the central autoinhibitory domain. Furthermore, the SRI domain is found to be essential for both di- and trimethylation when considering the full-length Set2 protein. These findings underscore the critical role of Set2 domains in modulating Set2 enzymatic activity.

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Published

2024-06-20

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Vol. 22 No. 2 (2024): Environmental and Experimental Biology

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Original Papers

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How to Cite

Nazir, S., Yasien, U., Ashraf, A., Ganie, S. A., & Bhat, A. W. (2024). Unravelling the role of Set2 protein domains in H3K36 methylation in Saccharomyces cerevisiae. Environmental and Experimental Biology, 22(2), 87-93. https://doi.org/10.22364/eeb.22.09