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Molecular and Cellular Biology, March 2001, p. 1737-1746, Vol. 21, No. 5
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.5.1737-1746.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

TFIIA Interacts with TFIID via Association with TATA-Binding Protein and TAF40

Susan M. Kraemer,1 Ryan T. Ranallo,2 Ryan C. Ogg,1 and Laurie A. Stargell1,*

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870,1 and Laboratory of Molecular Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-42552

Received 30 August 2000/Returned for modification 29 October 2000/Accepted 22 November 2000

TFIIA and TATA-binding protein (TBP) associate directly at the TATA element of genes transcribed by RNA polymerase II. In vivo, TBP is complexed with approximately 14 TBP-associated factors (TAFs) to form the general transcription factor TFIID. How TFIIA and TFIID communicate is not well understood. We show that in addition to making direct contacts with TBP, yeast TAF40 interacts directly and specifically with TFIIA. Mutational analyses of the Toa2 subunit of TFIIA indicate that loss of functional interaction between TFIIA and TAF40 results in conditional growth phenotypes and defects in transcription. These results demonstrate that the TFIIA-TAF40 interaction is important in vivo and indicate a functional role for TAF40 as a bridging factor between TFIIA and TFIID.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870. Phone: (970) 491-5068. Fax: (970) 491-0494. E-mail: lstargel{at}lamar.colostate.edu.

Molecular and Cellular Biology, March 2001, p. 1737-1746, Vol. 21, No. 5
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.5.1737-1746.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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