The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain

  1. Lawrence C. Myers1,3,
  2. Claes M. Gustafsson1,3,
  3. David A. Bushnell1,
  4. Mary Lui2,
  5. Hediye Erdjument-Bromage2,
  6. Paul Tempst2, and
  7. Roger D. Kornberg1,4
  1. 1Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5400 USA; 2Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 USA

Abstract

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.

Keywords

Footnotes

  • 3 These authors contributed equally to this work.

  • 4 Corresponding author.

  • E-MAIL kornberg{at}stanford.edu; FAX (415) 723-8464.

    • Received August 26, 1997.
    • Accepted October 27, 1997.
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