title: MES-4: an autosome-associated histone methyltransferase that participates in silencing the X chromosomes in the C. elegans germ line.
abstract: Germ cell development in C. elegans requires that the X chromosomes be globally silenced during mitosis and early meiosis. We previously found that the nuclear proteins MES-2, MES-3, MES-4 and MES-6 regulate the different chromatin states of autosomes versus X chromosomes and are required for germline viability. Strikingly, the SET-domain protein MES-4 is concentrated on autosomes and excluded from the X chromosomes. Here, we show that MES-4 has histone H3 methyltransferase (HMT) activity in vitro, and is required for histone H3K36 dimethylation in mitotic and early meiotic germline nuclei and early embryos. MES-4 appears unlinked to transcription elongation, thus distinguishing it from other known H3K36 HMTs. Based on microarray analysis, loss of MES-4 leads to derepression of X-linked genes in the germ line. We discuss how an autosomally associated HMT may participate in silencing genes on the X chromosome, in coordination with the direct silencing effects of the other MES proteins.
authors.affiliation: Department of Biology, Indiana University, Bloomington, IN 47405, USA. lbender@indiana.edu
authors.forename: Laurel B
authors.initials: LB
authors.lastname: Bender
authors.forename: Jinkyo
authors.initials: J
authors.lastname: Suh
authors.forename: Coleen R
authors.initials: CR
authors.lastname: Carroll
authors.forename: Youyi
authors.initials: Y
authors.lastname: Fong
authors.forename: Ian M
authors.initials: IM
authors.lastname: Fingerman
authors.forename: Scott D
authors.initials: SD
authors.lastname: Briggs
authors.forename: Ru
authors.initials: R
authors.lastname: Cao
authors.forename: Yi
authors.initials: Y
authors.lastname: Zhang
authors.forename: Valerie
authors.initials: V
authors.lastname: Reinke
authors.forename: Susan
authors.initials: S
authors.lastname: Strome
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000196:embryology* / Q000201:enzymology / Q000235:genetics; D029742:Caenorhabditis elegans Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000201:enzymology; D047108:Embryonic Development / Q000235:genetics; D005260:Female; D018507:Gene Expression Regulation, Developmental; D020868:Gene Silencing; D005854:Germ Cells / Q000166:cytology / Q000378:metabolism*; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000378:metabolism; D008297:Male; D008540:Meiosis / Q000235:genetics; D008745:Methylation; D008938:Mitosis / Q000235:genetics; D009687:Nuclear Proteins / Q000378:metabolism; D020411:Oligonucleotide Array Sequence Analysis; D063146:Polycomb-Group Proteins; D011496:Protein Methyltransferases; D014158:Transcription, Genetic; D014960:X Chromosome / Q000235:genetics* / Q000378:metabolism
chemical_list: D029742:Caenorhabditis elegans Proteins; D006657:Histones; C098864:Mes-3 protein, C elegans; C449639:Mes-4 protein, C elegans; D009687:Nuclear Proteins; D063146:Polycomb-Group Proteins; C113414:mes-2 protein, C elegans; C113415:mes-6 protein, C elegans; D000076983:Histone Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase