title: Methionine adenosyltransferase II-dependent histone H3K9 methylation at the COX-2 gene locus.
abstract: BACKGROUND
  MATII biosynthesizes AdoMet, which supplies methyl group for methylation of molecules, including histone.
  
  
  RESULTS
  MATII interacts with histone methyltransferase SETDB1 and inhibits COX-2 gene expression.
  
  
  CONCLUSIONS
  AdoMet synthesis and histone methylation are coupled on chromatin by a physical interaction of MATII and SETDB1 at the MafK target genes.
  
  
  CONCLUSIONS
  MATII may be important for both gene-specific and epigenome-wide regulation of histone methylation. Methionine adenosyltransferase (MAT) synthesizes S-adenosylmethionine (AdoMet), which is utilized as a methyl donor in transmethylation reactions involving histones. MATIIα, a MAT isozyme, serves as a transcriptional corepressor in the oxidative stress response and forms the AdoMet-integrating transcription regulation module, affecting histone methyltransferase activities. However, the identities of genes regulated by MATIIα or its associated methyltransferases are unclear. We show that MATIIα represses the expression of cyclooxygenase 2 (COX-2), encoded by Ptgs2, by specifically interacting with histone H3K9 methyltransferase SETDB1, thereby promoting the trimethylation of H3K9 at the COX-2 locus. We discuss both gene-specific and epigenome-wide functions of MATIIα.
authors.affiliation: Department of Biochemistry and Center for Regulatory Epigenome and Disease, Graduate School of Medicine, Tohoku University, Seiryo-machi 2-1, Sendai 980-8575, Japan.
authors.forename: Yohei
authors.initials: Y
authors.lastname: Kera
authors.forename: Yasutake
authors.initials: Y
authors.lastname: Katoh
authors.forename: Mineto
authors.initials: M
authors.lastname: Ohta
authors.forename: Mitsuyo
authors.initials: M
authors.lastname: Matsumoto
authors.forename: Teruko
authors.initials: T
authors.lastname: Takano-Yamamoto
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Igarashi
mesh_terms: D000818:Animals; D002460:Cell Line; D051546:Cyclooxygenase 2 / Q000235:genetics* / Q000378:metabolism; D004742:Enhancer Elements, Genetic; D004794:Enzyme Repression; D055785:Gene Knockdown Techniques; D020868:Gene Silencing; D051547:Heme Oxygenase-1 / Q000235:genetics; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics; D008716:Methionine Adenosyltransferase / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D051379:Mice; D020411:Oligonucleotide Array Sequence Analysis; D011499:Protein Processing, Post-Translational; D034741:RNA, Small Interfering / Q000235:genetics; D059467:Transcriptome
chemical_list: D006657:Histones; D008565:Membrane Proteins; D034741:RNA, Small Interfering; D051547:Heme Oxygenase-1; C496542:Hmox1 protein, mouse; C077623:Ptgs2 protein, mouse; D051546:Cyclooxygenase 2; D011495:Histone-Lysine N-Methyltransferase; C516239:SETDB1 protein, mouse; D008716:Methionine Adenosyltransferase
keywords: Chromatin Regulation; Cyclooxygenase (COX) Pathway; Heme Oxygenase; Histone Methylation; S-adenosylmethionine (AdoMet)
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