Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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The 80th Threonine Residue of Histone H3 Is Important for Maintaining HM Silencing in Saccharomyces cerevisiae

  • Soojin Yeom (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University) ;
  • Junsoo Oh (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University) ;
  • Donghyun Kim (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University) ;
  • Jung-Shin Lee (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University)
  • Received : 2023.10.23
  • Accepted : 2023.11.08
  • Published : 2024.01.28
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Abstract

Gene expression in eukaryotic cells is intricately regulated by chromatin structure and various factors, including histone proteins. In Saccharomyces cerevisiae, transcriptionally silenced regions, such as telomeres and homothallic mating (HM) loci, are essential for genome stability and proper cellular function. We firstly observed the defective HM silencing in alanine substitution mutant of 80th threonine residue of histone H3 (H3T80A). To identify which properties in the H3T80 residue are important for the HM silencing, we created several substitution mutants of H3T80 residue by considering the changed states of charge, polarity, and structural similarity. This study reveals that the structural similarity of the 80th position of H3 to the threonine residue, not the polarity and charges, is the most important thing for the transcriptional silencing in the HM loci.

Keywords

Acknowledgement

This work is supported by the National Research Foundation of Korea grants (NRF-2019H1A2A1075974 and RS-2023-00274760 to S.Y, NRF-2020R1A6A3A13077356 and NRF-2022R1A6A3A01087657 to J.O, NRF-2020R1I1A3072234 and NRF-2023R1A2C1003170 to J.L) and Ministry of Science and ICT, Korea (RS-2023-00260267).

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