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

• Published in: The Journal of biological chemistry Vol. 278; no. 10; pp. 8487 - 8493
• Main Authors: Roguev, Assen, Schaft, Daniel, Shevchenko, Anna, Aasland, Rein, Shevchenko, Andrej, Stewart, A Francis
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 07.03.2003
• Subjects: DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Histone-Lysine N-Methyltransferase; Histones - chemistry; Histones - metabolism; Ligases - chemistry; Ligases - metabolism; Lysine - metabolism; Mass Spectrometry; Methylation; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Schizosaccharomyces - metabolism; Transcription Factors - chemistry; Transcription Factors - metabolism; Ubiquitin-Conjugating Enzymes
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M209562200

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 ( l ittle i maginal d iscs). Thus, we infer that Set1C is highly conserved in eukaryotes but observe that its links to the proteome are not.