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J. Biol. Chem., Vol. 278, Issue 37, 34739-34742, September 12, 2003
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ACCELERATED PUBLICATIONS
The Paf1 Complex Is Essential for Histone Monoubiquitination by the Rad6-Bre1 Complex, Which Signals for Histone Methylation by COMPASS and Dot1p*
¶ || **
From the
Department of Biochemistry, Saint Louis
University School of Medicine, St. Louis, Missouri 63104, the
Department of Genetics, Washington University
School of Medicine, St. Louis, Missouri 63110, and
||Saint Louis University Cancer Center, Saint Louis
University School of Medicine, St. Louis, Missouri 63104
Monoubiquitination of histone H2B, catalyzed by Rad6-Bre1, is required for methylation of histone H3 on lysines 4 and 79, catalyzed by the Set1-containing complex COMPASS and Dot1p, respectively. The Paf1 protein complex, which associates with RNA polymerase II, is known to be required for these histone H3 methylation events. During the early elongation stage of transcription, the Paf1 complex is required for association of COMPASS with RNA polymerase II, but the role the Paf1 complex plays at the promoter has not been clear. We present evidence that the Paf1 complex is required for monoubiquitination of histone H2B at promoters. Strains deleted for several components of the Paf1 complex are defective in monoubiquitination of histone H2B, which results in the loss of methylation of lysines 4 and 79 of histone H3. We also show that Paf1 complex is required for the interaction of Rad6 and COMPASS with RNA polymerase II. Finally, we show that the Paf1 complex is required for Rad6-Bre1 catalytic activity but not for the recruitment of Rad6-Bre1 to promoters. Thus, in addition to its role during the elongation phase of transcription, the Paf1 complex appears to activate the function but not the placement of the Rad6-Bre1 ubiquitin-protein ligase at the promoters of active genes.
Received for publication, June 17, 2003 , and in revised form, July 21, 2003.
* This work was supported in part by grants from the American Cancer Society (RP69921801), the National Institutes of Health (1R01CA089455), and a Mallinckrodt Foundation Award (to A. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ Supported by the James S. McDonnell Foundation.
** A scholar of the Leukemia and Lymphoma Society. To whom correspondence should be addressed: Saint Louis University School of Medicine, Dept. of Biochemistry, 1402 S. Grand Blvd., St. Louis, MO 63104. Tel.: 314-577-8137; Fax: 314-268-5737; E-mail: shilatia{at}slu.edu.
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