title: [Effects of histone H3 K4L and K36L mutations on the cell growth and the transcription of GAL1, SSA3 and PHO5 in Saccharomyces cerevisiae].
abstract: Post-translational modifications of histones, such as acetylation and methylation, have a pivotal role in regulating gene expression and cell growth. To elucidate the different roles and importance of H3K4 and H3K36 modifications in expression of inducible genes such as Cal1, SSA3, PHO5 and the growth of yeast cell, we constructed three different yeast mutant strains carrying mutations of lysine 4, 36, or both to leucine in the histone H3 tail. Real-time PCR and sensitive assay under the conditions of high temperature, NaCl, caffeine, 6-AU, or other conditions were carried out to characterize the effects of these mutations on cell growth and transcription levels of GAL1, SSA3 and PHO5. The results showed that three histone methylation mutants exhibited more severe growth defects and slower activation of GAL1, SSA3 and PHO5 than those of wild type; H3K4L/H3K36L double mutant strain D436 has the most severe phenotype. H3K4L mutants S4 exhibited more severe defects than those of H3K36L S36 mutants, especially at high temperature and high NaCl stresses. These results show that H3K4L and H3K36L are important for the growth and survival of yeast in unfavorable conditions, and that different mutations have different effects on the expression of single inducible gene, whereas the same mutation has different effects on the activation of different inducible genes in vivo. The post-translational modification of H3K4 is more important than H3K36 on the adaptation to harsh condition for yeast cell. The growth defects of histone mutant strains might arise from the slow activation of inducible gene essential for survival at harsh conditions.
authors.affiliation: 1. College of Life Science, Henan Normal University, Xinxiang 453007, China; 2. Key Laboratory for Microorganisms and Functional Molecules, University of Henan Province, Xinxiang 453007, China;
authors.forename: Fen
authors.initials: F
authors.lastname: Li
authors.affiliation: Ocean College of Hebei Agricultural University, Qinhuangdao 066003, China.
authors.forename: Jinghui
authors.initials: J
authors.lastname: Yang
authors.affiliation: College of Life Science, Henan Normal University, Xinxiang 453007, China.
authors.forename: Xiuli
authors.initials: X
authors.lastname: Wu
authors.affiliation: College of Life Science, Henan Normal University, Xinxiang 453007, China.
authors.forename: Weilin
authors.initials: W
authors.lastname: Zhang
authors.affiliation: College of Life Science, Henan Normal University, Xinxiang 453007, China.
authors.forename: Guanfeng
authors.initials: G
authors.lastname: Wang
authors.affiliation: College of Life Science, Henan Normal University, Xinxiang 453007, China.
authors.forename: Xiaojie
authors.initials: X
authors.lastname: Yue
mesh_terms: D000135:Acid Phosphatase / Q000235:genetics; D000222:Adaptation, Physiological / Q000235:genetics; D049109:Cell Proliferation; D005686:Galactokinase / Q000235:genetics; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics; D006657:Histones / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008745:Methylation; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000166:cytology* / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics*; D014158:Transcription, Genetic / Q000235:genetics*
chemical_list: D018840:HSP70 Heat-Shock Proteins; D006657:Histones; C090869:SSA3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C524219:GAL1 protein, S cerevisiae; D005686:Galactokinase; D000135:Acid Phosphatase; C488916:PHO5 protein, S cerevisiae