title: Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression.
abstract: Higher-order chromatin has been implicated in epigenetic gene control and in the functional organization of chromosomes. We have recently discovered mouse (Suv39h1) and human (SUV39H1) histone H3 lysine 9-selective methyltransferases (Suv39h HMTases) and shown that they modulate chromatin dynamics in somatic cells. We describe here the isolation, chromosomal assignment, and characterization of a second murine gene, Suv39h2. Like Suv39h1, Suv39h2 encodes an H3 HMTase that shares 59% identity with Suv39h1 but which differs by the presence of a highly basic N terminus. Using fluorescent in situ hybridization and haplotype analysis, the Suv39h2 locus was mapped to the subcentromeric region of mouse chromosome 2, whereas the Suv39h1 locus resides at the tip of the mouse X chromosome. Notably, although both Suv39h loci display overlapping expression profiles during mouse embryogenesis, Suv39h2 transcripts remain specifically expressed in adult testes. Immunolocalization of Suv39h2 protein during spermatogenesis indicates enriched distribution at the heterochromatin from the leptotene to the round spermatid stage. Moreover, Suv39h2 specifically accumulates with chromatin of the sex chromosomes (XY body) which undergo transcriptional silencing during the first meiotic prophase. These data are consistent with redundant enzymatic roles for Suv39h1 and Suv39h2 during mouse development and suggest an additional function of the Suv39h2 HMTase in organizing meiotic heterochromatin that may even impart an epigenetic imprint to the male germ line.
authors.affiliation: Research Institute of Molecular Pathology at The Vienna Biocenter, University of Vienna, A-1030 Vienna, Austria.
authors.forename: D
authors.initials: D
authors.lastname: O'Carroll
authors.forename: H
authors.initials: H
authors.lastname: Scherthan
authors.forename: A H
authors.initials: AH
authors.lastname: Peters
authors.forename: S
authors.initials: S
authors.lastname: Opravil
authors.forename: A R
authors.initials: AR
authors.lastname: Haynes
authors.forename: G
authors.initials: G
authors.lastname: Laible
authors.forename: S
authors.initials: S
authors.lastname: Rea
authors.forename: M
authors.initials: M
authors.lastname: Schmid
authors.forename: A
authors.initials: A
authors.lastname: Lebersorger
authors.forename: M
authors.initials: M
authors.lastname: Jerratsch
authors.forename: L
authors.initials: L
authors.lastname: Sattler
authors.forename: M G
authors.initials: MG
authors.lastname: Mattei
authors.forename: P
authors.initials: P
authors.lastname: Denny
authors.forename: S D
authors.initials: SD
authors.lastname: Brown
authors.forename: D
authors.initials: D
authors.lastname: Schweizer
authors.forename: T
authors.initials: T
authors.lastname: Jenuwein
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002478:Cells, Cultured; D002843:Chromatin / Q000235:genetics* / Q000378:metabolism; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004622:Embryo, Mammalian / Q000378:metabolism; D005347:Fibroblasts; D015870:Gene Expression; D005854:Germ Cells / Q000378:metabolism; D006367:HeLa Cells; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006801:Humans; D015151:Immunoblotting; D017404:In Situ Hybridization, Fluorescence; D008297:Male; D008780:Methyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D011496:Protein Methyltransferases; D012313:RNA / Q000378:metabolism; D012730:Sex Chromosomes / Q000378:metabolism; D013737:Testis / Q000033:anatomy & histology / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002843:Chromatin; D010750:Phosphoproteins; D012313:RNA; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase