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Nucleic Acids Research 2005 33(16):5045-5052; doi:10.1093/nar/gki825
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Published online 7 September 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Evidence that the Tfg1/Tfg2 dimer interface of TFIIF lies near the active center of the RNA polymerase II initiation complex

M. Angeles Freire-Picos1,2, Shankarling Krishnamurthy2, Zu-Wen Sun2 and Michael Hampsey2,*

1Departamento de Bioloxía Celular e Molecular, Area de Bioquímica e Bioloxía Molecular Campus da Zapateira S/N 1071 A Coruña, Spain 2Department of Biochemistry, Division of Nucleic Acids Enzymology, UMDNJ-Robert Wood Johnson Medical School Piscataway, NJ 08854, USA

*To whom correspondence should be addressed. Tel: +1 732 235 5888; Fax: +1 732 235 5889; Email: michael.hampsey{at}umdnj.edu

Received July 27, 2005. Revised August 23, 2005. Accepted August 23, 2005.

The ssu71 alleles of the TFG1 gene, which encodes the largest subunit of TFIIF, were isolated as suppressors of a TFIIB defect that affects the accuracy of transcription start site selection in the yeast Saccharomyces cerevisiae. Here we report that ssu71-1 also suppresses the cell growth and start site defects associated with an altered form of the Rpb1 subunit of RNA polymerase II (RNAP II). The ssu71-1 and ssu71-2 alleles were cloned and found to encode single amino acid replacements of glycine-363, either glycine to aspartic acid (G363D) or glycine to arginine (G363R). Two other charged replacements, G363E and G363K, were constructed by site-directed mutagenesis and suppress both TFIIB E62K and Rpb1 N445S, whereas neither G363A nor G363P exhibited any effect. G363 is phylogenetically conserved and its counterpart in human TFIIF (RAP74 G112) is located within the RAP74/RAP30 dimerization domain. We propose that the TFIIF dimerization domain is located in proximity to the B-finger of TFIIB near the active center of RNAP II where the TFIIB–TFIIF–RNAP II interface plays a key role in start site selection.

Present address: Zu-Wen Sun, Department of Biochemistry, Vanderbilt University School of Medicine, 613C Light Hall, Nashville, TN 37232, USA


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