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Molecular and Cellular Biology, March 2005, p. 2117-2129, Vol. 25, No. 6
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.6.2117-2129.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Structural and Functional Characterization of PC2 and RNA Polymerase II-Associated Subpopulations of Metazoan Mediator

Sohail Malik,1* Hwa Jin Baek,1 Weizhen Wu,1 and Robert G. Roeder1

Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, New York1

Received 12 July 2004/ Returned for modification 10 August 2004/ Accepted 6 December 2004

The coactivator complexes TRAP/SMCC and PC2 represent two forms of Mediator. To further understand the implications of the heterogeneity of the cellular Mediator populations for regulation of RNA polymerase II (Pol II) transcription, we used a combination of affinity and conventional chromatographic methods. Our analysis revealed a spectrum of complexes, including some containing significant proportions of Pol II. Interestingly, the subunit composition of the Pol II-associated Mediator population resembled that of PC2 more closely than that of the larger TRAP/SMCC complex. In in vitro transcription assays reconstituted from homogeneous preparations of general transcription factors, Mediator-associated Pol II displayed a greater specific activity (relative to that of standard Pol II) in activator-independent (basal) transcription in addition to the previously described effects of Mediator on activator-dependent transcription. Purified PC2 complex also stimulated basal activity under these conditions. Immobilized template assays in which activator-recruited preinitiation complexes were allowed to undergo one cycle of transcription revealed partial disruption of Mediator that resulted in a PC2-like complex being retained in the scaffold. This result implies that PC2 could originate as a result of a normal cellular process. Our results are thus consistent with a dynamic nature of the Mediator complex and further extend the functional similarities between Saccharomyces cerevisiae and metazoan Mediator complexes.

* Corresponding author. Mailing address: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Ave., #166, New York, NY 10021. Phone: (212) 327-7623. Fax: (212) 327-7949. E-mail: maliks{at}rockefeller.edu.

Molecular and Cellular Biology, March 2005, p. 2117-2129, Vol. 25, No. 6
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.6.2117-2129.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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