title: Different roles of histone H3 lysine 4 methylation in chromatin maintenance.
abstract: Histone H3 methyltransferases are involved in the epigenetic control of transcription and heterochromatin maintenance. In Saccharomyces cerevisiae, deletion of a histone H3 methyltransferase SET1 leads to the induction of a subset of stress responsive genes in a Rad53 dependent manner. This type of induction was observed only in the absence of SET1 and not in the absence of other histone methyltransferases, SET2 or DOT1. We show that the increased expression of the stress responsive genes results from a lack of histone H3 lysine (K) 4 methylation. The loss of mono-methylation on H3 K4 is necessary to increase the expression of the stress responsive genes, while the loss of di- or tri-methylation induced by deletion of either RRM domain of Set1 or the upstream effector molecules hardly affected their expression. These results suggest that mono- and multiple methylation of H3 K4 have different roles. The mono-methylation of H3 K4 might be required for the global integrity of chromatin structure, which is normally monitored by the Rad53 dependent chromatin surveillance system.
authors.affiliation: College of Pharmacy Sungkyunkwan University, 300 Cheoncheon-dong, Jangan-gu, Suwon, Gyeonggi-do 440-746, South Korea.
authors.forename: Ja-Hwan
authors.initials: JH
authors.lastname: Seol
authors.forename: Hye-Jin
authors.initials: HJ
authors.lastname: Kim
authors.forename: Yong-Jin
authors.initials: YJ
authors.lastname: Yang
authors.forename: Seong-Tae
authors.initials: ST
authors.lastname: Kim
authors.forename: Hong-Duk
authors.initials: HD
authors.lastname: Youn
authors.forename: Jeong-Whan
authors.initials: JW
authors.lastname: Han
authors.forename: Hyang-Woo
authors.initials: HW
authors.lastname: Lee
authors.forename: Eun-Jung
authors.initials: EJ
authors.lastname: Cho
mesh_terms: D018797:Cell Cycle Proteins / Q000378:metabolism; D064447:Checkpoint Kinase 2; D002843:Chromatin / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000502:physiology; D044127:Epigenesis, Genetic; D005656:Fungal Proteins / Q000737:chemistry; D006570:Heterochromatin / Q000737:chemistry; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D008780:Methyltransferases / Q000502:physiology; D016296:Mutagenesis; D009687:Nuclear Proteins / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism / Q000502:physiology; D014157:Transcription Factors / Q000502:physiology
chemical_list: D018797:Cell Cycle Proteins; D002843:Chromatin; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D006570:Heterochromatin; D006657:Histones; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D008780:Methyltransferases; C448996:Set2 protein, S cerevisiae; C416235:Dot1 protein, S cerevisiae; D011495:Histone-Lysine N-Methyltransferase; C411250:SET1 protein, S cerevisiae; D064447:Checkpoint Kinase 2; D017346:Protein Serine-Threonine Kinases; C067022:RAD53 protein, S cerevisiae; D008239:Lysine