This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhao, X.
Right arrow Articles by Herr, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhao, X.
Right arrow Articles by Herr, W.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2003, p. 8152-8160, Vol. 23, No. 22
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.22.8152-8160.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Role of the Inhibitory DNA-Binding Surface of Human TATA-Binding Protein in Recruitment of Human TFIIB Family Members

Xuemei Zhao and Winship Herr*

Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

Received 25 March 2003/ Returned for modification 30 April 2003/ Accepted 22 July 2003

TATA box recognition by TATA-binding protein (TBP) is a key step in transcriptional initiation complex assembly on TATA-box-containing RNA polymerase (Pol) II and III promoters. This process is inhibited by the inhibitory DNA-binding (IDB) surface on the human TBP core domain (TBPCORE) and is stimulated by promoter-specific basal transcription factors, such as two human TFIIB family members, the Pol II factor TFIIB and the Pol III factor Brf2, which is required for transcription from TATA-box-containing Pol III promoters. In contrast, the third TFIIB family member, Brf1, which is required for transcription from TATA-less Pol III promoters, does not stimulate TBP binding to the TATA box. We show here that in addition to its role in regulating TBP binding to a TATA box, the TBP IDB surface is unexpectedly involved in TBP association with all three TFIIB family members. Interestingly, the loss of IDB function has specific and diverse effects on each TFIIB family member. Indeed, the IDB and prototypical TFIIB contact surfaces of TBP, which lie on opposite sides of the TBPCORE, cooperate to form the wild-type TFIIB-TBP-TATA box complex. These results reveal how, through differential usage of opposite surfaces of the TBPCORE, TBP can achieve versatility in the assembly of Pol II and Pol III promoter complexes with TFIIB family proteins.

* Corresponding author. Mailing address: Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724. Phone: (516) 367-6909. Fax: (516) 367-6919. E-mail: herr{at}cshl.edu.

Molecular and Cellular Biology, November 2003, p. 8152-8160, Vol. 23, No. 22
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.22.8152-8160.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chang, P.-J., Shedd, D., Miller, G. (2008). A Mobile Functional Region of Kaposi's Sarcoma-Associated Herpesvirus ORF50 Protein Independently Regulates DNA Binding and Protein Abundance. J. Virol. 82: 9700-9716 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»