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Originally published In Press as doi:10.1074/jbc.M209562200 on December 17, 2002

J. Biol. Chem., Vol. 278, Issue 10, 8487-8493, March 7, 2003
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High Conservation of the Set1/Rad6 Axis of Histone 3 Lysine 4 Methylation in Budding and Fission Yeasts*

Assen RoguevDagger §, Daniel SchaftDagger §, Anna Shevchenko, Rein Aasland||**, Andrej Shevchenko, and A. Francis StewartDagger Dagger Dagger

From Dagger  BIOTEC, Technische Universitaet Dresden, c/o Max Planck Institute for Molecular Cell Biology and Genetics and the  Max Planck Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, D-01307 Dresden, Germany and the || Department of Molecular Biology, University of Bergen, Thromoehlenstrasse 55, N-5020 Bergen, Norway

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. cerevisiae findings 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.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

** Supported by Grant 146652/431 from the Norwegian Research Council.

Dagger Dagger To whom correspondence should be addressed. E-mail: stewart@mpi-cbg.de.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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