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1 Department of Structural Biology, Stanford University
School of Medicine, Stanford, California 94305-5400 USA;
2 Molecular Biology Program, Memorial Sloan-Kettering Cancer
Center, New York, New York 10021 USA
Mediator was resolved from yeast as a multiprotein complex on the
basis of its requirement for transcriptional activation in a fully
defined system. Three groups of mediator polypeptides could be
distinguished: the products of five SRB genes, identified as
suppressors of carboxy-terminal domain (CTD)-truncation mutants; products of four genes identified as global repressors; and six members
of a new protein family, termed Med, thought to be primarily responsible for transcriptional activation. Notably absent from the
purified mediator were Srbs 8, 9, 10, and 11, as well as members of the
SWI/SNF complex. The CTD was required for function of
mediator in vitro, in keeping with previous indications of involvement of the CTD in transcriptional activation in vivo. Evidence for human
homologs of several mediator proteins, including Med7, points to
similar mechanisms in higher cells.
[Key Words: RNA polymerase II holoenzyme; transcription; CTD; Saccharomyces cerevisiae]
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