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(Received for publication, February 27, 1997, and in revised form, July 20, 1997)
From the Affinity chromatography on columns containing the
immobilized monomeric transcriptional elongation factor TFIIS or the
essential large subunit, Elongin A, of the trimeric elongation factor,
Elongin, was used to purify a human RNA polymerase II holoenzyme from
HeLa whole cell extract. This holoenzyme contained
nearstoichiometric amounts of all the general transcription
factors, TFIIB, TFIID (TBP + TAFIIs), TFIIE, TFIIF,
and TFIIH, required to accurately initiate transcription in
vitro at the adenovirus major late promoter. It behaved as a
large complex, slightly smaller than 70 S ribosomes, during gel
filtration chromatography, and contained nearly half the TFIID that was
present in the extract used for the affinity chromatography. It also
contained the cyclin-dependent kinase CDK8, a human
homologue of the Saccharomyces cerevisiae holoenzyme subunit SRB10, and many other polypeptides. Efficient interaction of
holoenzyme with TFIIS or Elongin A required only the amino-terminal region of either protein. These regions are similar in amino acid sequence but dispensable for TFIIS or Elongin to regulate elongation in vitro by highly purified RNA polymerase II. The
transcriptional activators GAL4-VP16 and GAL4-Sp1 activated
transcription in vitro by purified holoenzyme in the
absence of any additional factors.
Volume 272, Number 39,
Issue of September 26, 1997
pp. 24563-24571
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Banting and Best Department of Medical
Research and Department of Molecular and Medical Genetics, University
of Toronto, Toronto, Ontario M5G 1L6, Canada and the ¶ Program
in Molecular and Cell Biology, Oklahoma Medical Research Foundation,
Oklahoma City, Oklahoma 73104
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