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Nucleic Acids Research 2005 33(17):5426-5436; doi:10.1093/nar/gki850
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Published online 22 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

Mutational analysis of BTAF1–TBP interaction: BTAF1 can rescue DNA-binding defective TBP mutants

Marcin P. Klejman, Xuemei Zhao1, Frederik M. A. van Schaik, Winship Herr1 and H. Th. Marc Timmers*

Department of Physiological Chemistry, Division of Biomedical Genetics, University Medical Center Utrecht Universiteitsweg 100, 3584 CG Utrecht, The Netherlands 1Cold Spring Harbor Laboratory Cold Spring Harbor, NY 11724, USA

*To whom correspondence should be addressed. Tel: +31 30 253 8981; Fax: + 31 30 253 9035; Email: h.t.m.timmers{at}med.uu.nl

Received June 26, 2005. Revised September 2, 2005. Accepted September 2, 2005.

The BTAF1 transcription factor interacts with TATA-binding protein (TBP) to form the B–TFIID complex, which is involved in RNA polymerase II transcription. Here, we present an extensive mapping study of TBP residues involved in BTAF1 interaction. This shows that residues in the concave, DNA-binding surface of TBP are important for BTAF1 binding. In addition, BTAF1 interacts with residues in helix 2 on the convex side of TBP as assayed in protein–protein and in DNA-binding assays. BTAF1 drastically changes the TATA-box binding specificity of TBP, as it is able to recruit DNA-binding defective TBP mutants to both TATA-containing and TATA-less DNA. Interestingly, other helix 2 interacting factors, such as TFIIA and NC2, can also stabilize mutant TBP binding to DNA. In contrast, TFIIB which interacts with a distinct surface of TBP does not display this activity. Since many proteins contact helix 2 of TBP, this provides a molecular basis for mutually exclusive TBP interactions and stresses the importance of this structural element for eukaryotic transcription.

Present addresses: Marcin P. Klejman, Department of Molecular Biology, International Institute of Molecular and Cell Biology, ul. Ks. Trojdena 4, 02-109 Warsaw, Poland

Xuemei Zhao, Proteomics, Department of Molecular Profiling, Merck Research Laboratories, Rahway, NJ 07065, USA

Winship Herr, Center for Integrative Genomics, University of Lausanne, CH-1015 Lausanne, Switzerland


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