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Molecular and Cellular Biology, February 2005, p. 945-957, Vol. 25, No. 3
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.3.945-957.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mapping and Functional Characterization of the TAF11 Interaction with TFIIA

M. M. Robinson, G. Yatherajam, R. T. Ranallo, A. Bric, M. R. Paule, and L. A. Stargell^*

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado

Received 20 May 2004/ Returned for modification 28 October 2004/ Accepted 5 November 2004

TFIIA interacts with TFIID via association with TATA binding protein (TBP) and TBP-associated factor 11 (TAF11). We previously identified a mutation in the small subunit of TFIIA (toa2-I27K) that is defective for interaction with TAF11. To further explore the functional link between TFIIA and TAF11, the toa2-I27K allele was utilized in a genetic screen to isolate compensatory mutants in TAF11. Analysis of these compensatory mutants revealed that the interaction between TAF11 and TFIIA involves two distinct regions of TAF11: the highly conserved histone fold domain and the N-terminal region. Cells expressing a TAF11 allele defective for interaction with TFIIA exhibit conditional growth phenotypes and defects in transcription. Moreover, TAF11 imparts changes to both TFIIA-DNA and TBP-DNA contacts in the context of promoter DNA. These alterations appear to enhance the formation and stabilization of the TFIIA-TBP-DNA complex. Taken together, these studies provide essential information regarding the molecular organization of the TAF11-TFIIA interaction and define a mechanistic role for this association in the regulation of gene expression in vivo.

Present address: Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104.

Present address: Walter Reed Army Institute of Research, Division of Communicable Diseases and Immunology, Department of Enteric Infections, Silver Spring, MD 20910.

Present address: Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724.

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