Mutational analysis of BTAF1-TBP interaction: BTAF1 can rescue DNA-binding defective TBP mutants
| العنوان: | Mutational analysis of BTAF1-TBP interaction: BTAF1 can rescue DNA-binding defective TBP mutants |
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| المؤلفون: | Marcin P. Klejman, Xuemei Zhao, Frederik M. A. van Schaik, H. Th. Marc Timmers, Winship Herr |
| المصدر: | Nucleic acids research, vol. 33, no. 17, pp. 5426-5436 Nucleic Acids Research |
| بيانات النشر: | Oxford University Press (OUP), 2005. |
| سنة النشر: | 2005 |
| مصطلحات موضوعية: | DNA Mutational Analysis, genetic processes, information science, RNA polymerase II, macromolecular substances, Article, Transcription (biology), Binding Sites, DNA/metabolism, 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, Genetics, Binding site, TATA-Binding Protein Associated Factors, biology, TATA-Box Binding Protein, Eukaryotic transcription, DNA, Phosphoproteins, Molecular biology, enzymes and coenzymes (carbohydrates), Transcription Factor TFIIA, Transcription Factor TFIID, health occupations, biology.protein, Biophysics, Transcription factor II B, Transcription factor II A, Transcription Factors |
| الوصف: | 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. |
| وصف الملف: | application/pdf |
| تدمد: | 1362-4962 0305-1048 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65352b4941b04e9f40b11ae60c7c8489Test https://doi.org/10.1093/nar/gki850Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....65352b4941b04e9f40b11ae60c7c8489 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 13624962 03051048 |
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