serval:BIB_414353841D38
Mutational analysis of BTAF1-TBP interaction: BTAF1 can rescue DNA-binding defective TBP mutants.
10.1093/nar/gki850
16179647
Klejman
M.P.
author
Zhao
X.
author
van Schaik
F.M.
author
Herr
W.
author
Timmers
H.T.
author
article
2005
Nucleic acids research
1362-4962
0305-1048
journal
33
17
5426-5436
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.
Binding Sites
DNA/metabolism
DNA Mutational Analysis
Humans
Phosphoproteins/metabolism
TATA Box
TATA-Binding Protein Associated Factors/metabolism
TATA-Box Binding Protein/chemistry
TATA-Box Binding Protein/genetics
TATA-Box Binding Protein/metabolism
Transcription Factor TFIIA/metabolism
Transcription Factor TFIID/metabolism
Transcription Factors/metabolism
eng
60_published
true
peer-reviewed
University of Lausanne
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