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J Biol Chem, Vol. 275, Issue 2, 1351-1356, January 14, 2000
From the Institute of Medical Biochemistry, Göteborg
University, P. O. Box 440, 405 30 Göteborg, Sweden
We have purified the RNA polymerase II holoenzyme
from Schizosaccharomyces pombe to near homogeneity. The
Mediator complex is considerably smaller than its counterpart in
Saccharomyces cerevisiae, containing only nine polypeptides
larger than 19 kDa. Five of these Mediator subunits have been
identified as the S. pombe homologs to Rgr1, Srb4, Med7,
and Nut2 found in S. cerevisiae and the gene product of a
previously uncharacterized open reading frame, PMC2, with
no clear homologies to any described protein. The presence of Mediator
in a S. pombe RNA polymerase II holoenzyme stimulated
phosphorylation of the C-terminal domain by TFIIH purified from
S. pombe. This stimulation was species-specific, because S. pombe Mediator could not stimulate TFIIH purified from
S. cerevisiae. We suggest that the overall structure and
mechanism of the Mediator is evolutionary conserved. The subunit
composition, however, has evolved to respond properly to physiological signals.
Purification and Characterization of RNA Polymerase II Holoenzyme
from Schizosaccharomyces pombe*
, and
*
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.
Supported by Grants 3967 and 10435 from the Swedish Medical Research
Council, the Swedish Research Council for Engineering Sciences, the
Swedish Foundation for Strategic Research, the Knut and Alice
Wallenberg Foundation, and the IngaBritt and Arne Lundberg Foundation.
§
Supported by grants from the Swedish Cancer Society (project 3947),
the Magn. Bergvalls Foundation, the Swedish Society for Medical
Research, the Swedish Foundation for Strategic Research, and the
Swedish Society of Medicine. To whom correspondence should be
addressed. Tel.: 46 31 7733470; Fax: 46 31 416108; E-mail: claes.
gustafsson@medkem.gu.se.
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