Mutational analysis of BTAF1-TBP interaction: BTAF1 can rescue DNA-binding defective TBP mutants

Klejman, M. P., Zhao, X. M., van Schaik, F. M. A., Herr, W., Timmers, H. T. M. (2005) Mutational analysis of BTAF1-TBP interaction: BTAF1 can rescue DNA-binding defective TBP mutants. Nucleic Acids Research, 33 (17). pp. 5426-5436. ISSN 0305-1048

[thumbnail of Paper]
Preview
PDF (Paper)
Mutational analysis of BTAF1.pdf - Published Version

Download (2MB) | Preview

Abstract

The BTAF1 transcription factor interacts with TATA-binding protein (TBP) to form the B-TFIID complex, which is involved in RNA polymerase II transcription. Here, we present an extensive mapping study of TBP residues involved in BTAF1 interaction. This shows that residues in the concave, DNA-binding surface of TBP are important for BTAF1 binding. In addition, BTAF1 interacts with residues in helix 2 on the convex side of TBP as assayed in protein-protein and in DNA-binding assays. BTAF1 drastically changes the TATA-box binding specificity of TBP, as it is able to recruit DNA-binding defective TBP mutants to both TATA-containing and TATA-less DNA. Interestingly, other helix 2 interacting factors, such as TFIIA and NC2, can also stabilize mutant TBP binding to DNA. In contrast, TFIIB which interacts with a distinct surface of TBP does not display this activity. Since many proteins contact helix 2 of TBP, this provides a molecular basis for mutually exclusive TBP interactions and stresses the importance of this structural element for eukaryotic transcription.

Item Type: Paper
Uncontrolled Keywords: RNA polymerase II protein family member transcription factor basal transcription saccharomyces cereveseae crystal structure in vivo in-vivo MOT1 complex yeast
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > annotation > map annotation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: CSHL Librarian
Date: 2005
Date Deposited: 12 Jan 2012 17:38
Last Modified: 08 May 2018 20:07
PMCID: PMC1236718
Related URLs:
URI: https://repository.cshl.edu/id/eprint/22624

Actions (login required)

Administrator's edit/view item Administrator's edit/view item