| Title: | Positive Charge of Arginine Residues on Histone H4 Tail Is Required for Maintenance of Mating Type in Saccharomyces cerevisiae |
| Author(s): | Yeom S; Oh J; Lee EJ; Lee JS; |
| Address: | "Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea. Critical Zone Frontier Research Laboratory, Kangwon National University, Chuncheon 24341, Republic of Korea. Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon 24341, Republic of Korea. Department of Genetic Engineering and Graduate School of Biotechnology, College of Life Sciences, Kyung Hee University, Yongin 17104, Republic of Korea" |
| ISSN/ISBN: | 1738-8872 (Electronic) 1017-7825 (Linking) |
| 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" |
| Keywords: | "Arginine/*chemistry Gene Silencing/drug effects/*physiology Genes, Mating Type, Fungal/*genetics Histones/*chemistry/genetics Lysine/chemistry Saccharomyces cerevisiae/*genetics/physiology Telomere/*chemistry HM silencing Saccharomyces cerevisiae arginine;" |
| Notes: | "MedlineYeom, Soojin Oh, Junsoo Lee, Eun-Jin Lee, Jung-Shin eng Korea (South) 2018/09/05 J Microbiol Biotechnol. 2018 Sep 28; 28(9):1573-1579. doi: 10.4014/jmb.1807.07044" |
