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Originally published In Press as doi:10.1074/jbc.M206946200 on December 4, 2002

J. Biol. Chem., Vol. 278, Issue 6, 3831-3839, February 7, 2003
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Functional Interactions within Yeast Mediator and Evidence of Differential Subunit Modifications*

Darius BalciunasDagger §, Magnus Hallberg||, Stefan Björklund||, and Hans RonneDagger **

From the Dagger  Department of Plant Biology, Swedish University of Agricultural Sciences, Uppsala Genetic Center, Box 7080, S-75007 Uppsala, Sweden, § Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, S-75123 Uppsala, Sweden, and the || Department of Medical Biochemistry and Biophysics, Umeå University, S-90187 Umeå, Sweden

It is possible to recruit RNA polymerase II to a target promoter and, thus, activate transcription by fusing Mediator subunits to a DNA binding domain. To investigate functional interactions within Mediator, we have tested such fusions of the lexA DNA binding domain to Med1, Med2, Gal11, Srb7, and Srb10 in wild type, med1, med2, gal11, sin4, srb8, srb10, and srb11 strains. We found that lexA-Med2 and lexA-Gal11 are strong activators that are independent of all Mediator subunits tested. lexA-Srb10 is a weak activator that depends on Srb8 and Srb11. lexA-Med1 and lexA-Srb7 are both cryptic activators that become active in the absence of Srb8, Srb10, Srb11, or Sin4. An unexpected finding was that lexA-VP16 differs from Gal4-VP16 in that it is independent of the activator binding Mediator module. Both lexA-Med1 and lexA-Srb7 are stably associated with Med4 and Med8, which suggests that they are incorporated into Mediator. Med4 and Med8 exist in two mobility forms that differ in their association with lexA-Med1 and lexA-Srb7. Within purified Mediator, Med4 is present as a phosphorylated lower mobility form. Taken together, these results suggest that assembly of Mediator is a multistep process that involves conversion of both Med4 and Med8 to their low mobility forms.

* This work was supported by grants from the Swedish Research Council and the Swedish Cancer Society (to H. R. and S. B.), the Kempe Foundation (to M. H.), and the Swedish Foundation for Strategic Research and the Human Frontier Science Program (to S. B.).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.

Present address: Dept. of Genetics, Cell Biology, and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church St. S. E., Minneapolis, MN 55455.

** To whom correspondence should be addressed: Dept. of Plant Biology, Swedish University of Agricultural Sciences, Box 7080, S-750 07 Uppsala, Sweden. Tel.: 46-18-673313; Fax: 46-18-673279; E-mail: Hans.Ronne@vbiol.slu.se.

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