title: High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation in budding and fission yeasts.
abstract: Histone 3 lysine 4 (H3 Lys(4)) methylation in Saccharomyces cerevisiae is mediated by the Set1 complex (Set1C) and is dependent upon ubiquitinylation of H2B by Rad6. Mutually exclusive methylation of H3 at Lys(4) or Lys(9) is central to chromatin regulation; however, S. cerevisiae lacks Lys(9) methylation. Furthermore, a different H3 Lys(4) methylase, Set 7/9, has been identified in mammals, thereby questioning the relevance of the S. cerevisiae findings for eukaryotes in general. We report that the majority of Lys(4) methylation in Schizosaccharomyces pombe, like in S. cerevisiae, is mediated by Set1C and is Rad6-dependent. S. pombe Set1C mediates H3 Lys(4) methylation in vitro and contains the same eight subunits found in S. cerevisiae, including the homologue of the Drosophila trithorax Group protein, Ash2. Three additional features of S. pombe Set1C each involve PHD fingers. Notably, the Spp1 subunit is dispensable for H3 Lys(4) methylation in budding yeast but required in fission yeast, and Sp_Set1C has a novel proteomic hyperlink to a new complex that includes the homologue of another trithorax Group protein, Lid (little imaginal discs). Thus, we infer that Set1C is highly conserved in eukaryotes but observe that its links to the proteome are not.
authors.affiliation: BIOTEC, Technische Universitaet Dresden, c/o Max Planck Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, Germany.
authors.forename: Assen
authors.initials: A
authors.lastname: Roguev
authors.forename: Daniel
authors.initials: D
authors.lastname: Schaft
authors.forename: Anna
authors.initials: A
authors.lastname: Shevchenko
authors.forename: Rein
authors.initials: R
authors.lastname: Aasland
authors.forename: Andrej
authors.initials: A
authors.lastname: Shevchenko
authors.forename: A Francis
authors.initials: AF
authors.lastname: Stewart
mesh_terms: D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008025:Ligases / Q000737:chemistry / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D013058:Mass Spectrometry; D008745:Methylation; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D012568:Schizosaccharomyces / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes
chemical_list: D004268:DNA-Binding Proteins; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D011495:Histone-Lysine N-Methyltransferase; C411250:SET1 protein, S cerevisiae; C471606:RAD6 protein, S cerevisiae; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases; D008239:Lysine