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Molecular and Cellular Biology, January 2000, p. 488-495, Vol. 20, No. 2
Service de Biochimie et de
Génétique Moléculaire, CEA/Saclay, F-91191
Gif-sur-Yvette Cedex, France
Received 9 July 1999/Returned for modification 2 September
1999/Accepted 13 October 1999
There is limited information on how eukaryotic RNA polymerases
(Pol) recognize their cognate preinitiation complex. We have characterized a polypeptide copurifying with yeast Pol III. This protein, C17, was found to be homologous to a mammalian protein described as a hormone receptor. Deletion of the corresponding gene,
RPC17, was lethal and its regulated extinction caused
a selective defect in transcription of class III genes in vivo. Two-hybrid and coimmunoprecipitation experiments indicated that C17 interacts with two Pol III subunits, one of which, C31, is important for the initiation reaction. C17 also interacted with TFIIIB70, the TFIIB-related component of TFIIIB. The
interaction domain was found to be in the N-terminal, TFIIB-like half
of TFIIIB70, downstream of the zinc ribbon and first imperfect
repeat. Although Pol II similarly interacts with TFIIB, it is notable
that C17 has no similarity to any Pol II subunit. The data indicate
that C17 is a novel specific subunit of Pol III which
participates together with C34 in the recruitment of Pol III by the
preinitiation complex.
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
A Novel Subunit of Yeast RNA Polymerase III
Interacts with the TFIIB-Related Domain of TFIIIB70

*
Corresponding author. Mailing address: Service de
Biochimie et de Génétique Moléculaire, CEA/Saclay,
F-91191 Gif-sur-Yvette Cedex, France. Phone: 33 1 69 08 22 36. Fax: 33 1 69 08 47 12. E-mail: sentenac{at}dsvidf.cea.fr.
Present address: Génétique des Interactions
Macromoléculaires, CNRS (URA 1300), Institut Pasteur, 75724 Paris
Cedex 15, France.
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