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J. Biol. Chem., Vol. 276, Issue 13, 10097-10102, March 30, 2001
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From the The Rpb4 and Rpb7 subunits of yeast RNA
polymerase II form a heterodimeric complex essential for
promoter-directed transcription initiation in a reconstituted system.
Results of template competition experiments indicate that the Rpb4-Rpb7
complex is not required for stable recruitment of polymerase to active
preinitiation complexes, suggesting that Rpb4-Rpb7 mediates an
essential step subsequent to promoter binding. Sequence and
structure-based alignments revealed a possible OB-fold
single-strand nucleic acid-binding motif in Rpb7. Purified
Rpb4-Rpb7 complex exhibited both single-strand DNA- and RNA-binding
activities, and a small deletion in the putative OB-fold nucleic
acid-binding surface of Rpb7 abolished binding activity without
affecting the stability of the Rpb4-Rpb7 complex or its ability to
associate with polymerase. The same mutation destroyed the
transcription activity of the Rpb4-Rpb7 complex. A separate
deletion elsewhere in the OB-fold motif of Rpb7 also blocked
transcription but did not affect nucleic acid binding, suggesting that
the OB-fold of Rpb7 mediates both DNA-protein and protein-protein
interactions required for productive initiation.
Dissociable Rpb4-Rpb7 Subassembly of RNA Polymerase II
Binds to Single-strand Nucleic Acid and Mediates a Post-recruitment
Step in Transcription Initiation*
,
, and**
Banting and Best Department of Medical
Research and Department of Medical Genetics and Microbiology, C. H. Best Institute, University of Toronto, Toronto, Ontario M5G 1L6, Canada
and the § Department of Biochemistry, Johns Hopkins
University, Baltimore, Maryland 21205
*
This work was supported in part by grants from the Medical
Research Council of Canada (MRC) (to A. M. E.) and by Grant GM50724 from the National Institutes of Health (NIH) (to M. H. S.).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.
Current address: Division of Molecular and Cellular
Mechanisms, NIH Center for Scientific Review, 6701 Rockledge Dr.,
Bethesda, MD 20892. Recipient of a Junior Faculty research award from
the American Cancer Society.
**
MRC Scientist. To whom correspondence should be addressed: Banting
and Best Dept. of Medical Research and Dept. of Medical Genetics and
Microbiology, C. H. Best Inst., University of Toronto, 112 College
St., Toronto, Ontario M5G 1L6, Canada. Tel.: 416-946-3436; Fax:
416-978-8528; E-mail: aled.edwards@utoronto.ca.
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