Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Positive Charge of Arginine Residues on Histone H4 Tail Is Required for Maintenance of Mating Type in Saccharomyces cerevisiae

  • Yeom, Soojin (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University) ;
  • Oh, Junsoo (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University) ;
  • Lee, Eun-Jin (Department of Genetic Engineering and Graduate School of Biotechnology, College of Life Sciences, Kyung Hee University) ;
  • Lee, Jung-Shin (Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University)
  • Received : 2018.07.24
  • Accepted : 2018.08.02
  • Published : 2018.09.28
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Abstract

Transcriptional gene silencing is regulated by the chromatin structure, which is by various factors including histones. Saccharomyces cerevisiae contains transcriptionally silenced regions such as telomeric regions and hidden mating (HM) loci. The positively-charged amino acids on the histone H4 tail were reported to be critical for the telomeric silencing in yeast, by interacting with Dot1, a specific methyltransferase for the $79^{th}$ lysine on histone H3. However, Dot1 did not affect gene silencing within HM loci, but whether the positively-charged amino acids on the H4 tail affect HM silencing has not been defined. To elucidate the function of the H4 tail on HM silencing, we created several MATa-type yeast strains bearing the substitution of arginine with alanine or lysine on the histone H4 tail and checked the sensitivity of MATa-type yeast to alpha pheromone. The arginine point mutants substituted by alanine (R17A, R19A, and R23A) did not show sensitivity to alpha pheromone, but only two arginine mutants substituted by lysine (R17K and R19K) restored the sensitivity to alpha pheromone-like wild type. These data suggested that the basic property of arginine at $17^{th}$ and $19^{th}$ positions in the histone H4 tail is critical for maintaining HM silencing, but that of the $23^{rd}$ arginine is not. Our data implicated that the positive charge of two arginine residues on the histone H4 tail is required for HM silencing in a manner independent of Dot1.

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References

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