title: Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena.
abstract: Studies into posttranslational modifications of histones, notably acetylation, have yielded important insights into the dynamic nature of chromatin structure and its fundamental role in gene expression. The roles of other covalent histone modifications remain poorly understood. To gain further insight into histone methylation, we investigated its occurrence and pattern of site utilization in Tetrahymena, yeast, and human HeLa cells. In Tetrahymena, transcriptionally active macronuclei, but not transcriptionally inert micronuclei, contain a robust histone methyltransferase activity that is highly selective for H3. Microsequence analyses of H3 from Tetrahymena, yeast, and HeLa cells indicate that lysine 4 is a highly conserved site of methylation, which to date, is the major site detected in Tetrahymena and yeast. These data document a nonrandom pattern of H3 methylation that does not overlap with known acetylation sites in this histone. In as much as H3 methylation at lysine 4 appears to be specific to macronuclei in Tetrahymena, we suggest that this modification pattern plays a facilitatory role in the transcription process in a manner that remains to be determined. Consistent with this possibility, H3 methylation in yeast occurs preferentially in a subpopulation of H3 that is preferentially acetylated.
authors.affiliation: Department of Biochemistry, University of Virginia Health Science Center, Charlottesville, VA 22908, USA.
authors.forename: B D
authors.initials: BD
authors.lastname: Strahl
authors.forename: R
authors.initials: R
authors.lastname: Ohba
authors.forename: R G
authors.initials: RG
authors.lastname: Cook
authors.forename: C D
authors.initials: CD
authors.lastname: Allis
mesh_terms: D000123:Acetyltransferases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D006367:HeLa Cells; D051548:Histone Acetyltransferases; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D008969:Molecular Sequence Data; D011496:Protein Methyltransferases; D011499:Protein Processing, Post-Translational; D029701:Saccharomyces cerevisiae Proteins; D013045:Species Specificity; D016808:Tetrahymena thermophila; D014158:Transcription, Genetic; D015003:Yeasts
chemical_list: D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D008239:Lysine