High Conservation of the Set1/Rad6 Axis of Histone 3 Lysine 4 Methylation in Budding and Fission Yeasts*

Histone 3 lysine 4 (H3 Lys4) 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 Lys4 or Lys9 is central to chromatin regulation; however, S. cerevisiae lacks Lys9 methylation. Furthermore, a different H3 Lys4 methylase, Set 7/9, has been identified in mammals, thereby questioning the relevance of the S. cerevisiaefindings for eukaryotes in general. We report that the majority of Lys4 methylation in Schizosaccharomyces pombe, like in S. cerevisiae, is mediated by Set1C and is Rad6-dependent. S. pombe Set1C mediates H3 Lys4 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 Lys4 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.

• Publication year

  2003

• Venue

  Journal of Biological Chemistry

• Publication date

  2003-03-07

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1074/JBC.M209562200PMID 12488447
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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