Nucleic Acids Research, 2003, Vol. 31, No. 4 1252-1260
© 2003 Oxford University Press
Proteinprotein interaction map for yeast TFIID
Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA and 1 Department of Pathobiology, Seattle Biomedical Research Institute, 4 Nickerson Street, Seattle, WA 98109, USA
*To whom correspondence should be addressed. Tel: +1 970 491 5068; Fax: +1 970 491 0494; Email: lstargel{at}lamar.colostate.edu
A major rate-limiting step in transcription initiation by RNA polymerase II is recognition and binding of the TATA element by the transcription factor TFIID. TFIID is composed of TATA binding protein (TBP) and approximately a dozen TBP-associated factors (TAFs). Emerging consensus regarding the role of TAFs is that TFIID assumes a gene specific activity that is regulated by interaction with other factors. In spite of many studies demonstrating the essential nature of TAFs in transcription, very little is known about the subunit contacts within TFIID. To understand fully the functional role of TAFs, it is imperative to define TAFTAF interactions and their topological arrangement within TFIID. We performed a systematic two-hybrid analysis using the 13 essential TAFs of the Saccharomyces cerevisiae TFIID complex and TBP. Specific interactions were defined for each component, and the biological significance of these interactions is supported by numerous genetic and biochemical studies. By combining the interaction profiles presented here, and the available studies utilizing specific TAFs, we propose a working hypothesis for the arrangement of components in the TFIID complex. Thus, these results serve as a foundation for understanding the overall architecture of yeast TFIID.
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