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Molecular and Cellular Biology, June 1999, p. 3951-3957, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A TATA-Binding Protein Mutant Defective for TFIID Complex Formation In Vivo

Ryan T. Ranallo,1 Kevin Struhl,2 and Laurie A. Stargell1,*

Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870,1 and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152

Received 16 November 1998/Returned for modification 22 December 1998/Accepted 26 February 1999

Using an intragenic complementation screen, we have identified a temperature-sensitive TATA-binding protein (TBP) mutant (K151L,K156Y) that is defective for interaction with certain yeast TBP-associated factors (TAFs) at the restrictive temperature. The K151L,K156Y mutant appears to be functional for RNA polymerase I (Pol I) and Pol III transcription, and it is capable of supporting Gal4-activated and Gcn4-activated transcription by Pol II. However, transcription from certain TATA-containing and TATA-less Pol II promoters is reduced at the restrictive temperature. Immunoprecipitation analysis of extracts prepared after culturing cells at the restrictive temperature for 1 h indicates that the K151L,K156Y derivative is severely compromised in its ability to interact with TAF130, TAF90, TAF68/61, and TAF25 while remaining functional for interaction with TAF60 and TAF30. Thus, a TBP mutant that is compromised in its ability to form TFIID can support the response to Gcn4 but is defective for transcription from specific promoters in vivo.

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

Molecular and Cellular Biology, June 1999, p. 3951-3957, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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