TATA‐binding protein promotes the selective formation of UV‐induced (6‐4)‐photoproducts and modulates DNA repair in the TATA box
Open accessAbstract
DNA-damage formation and repair are coupled to the structure and accessibility of DNA in chromatin. DNA damage may compromise protein binding, thereby affecting function. We have studied the effect of TATA-binding protein (TBP) on damage formation by ultraviolet light and on DNA repair by photolyase and nucleotide excision repair in yeast and in vitro. In vivo, selective and enhanced formation of (6-4)-photoproducts (6-4PPs) was found within the TATA boxes of the active SNR6 and GAL10 genes, engaged in transcription initiation by RNA polymerase III and RNA polymerase II, respectively. Cyclobutane pyrimidine dimers (CPDs) were generated at the edge and outside of the TATA boxes, and in the inactive promoters. The same selective and enhanced 6-4PP formation was observed in a TBP-TATA complex in vitro at sites where crystal structures revealed bent DNA. We conclude that similar DNA distortions occur in vivo when TBP is part of the initiation complexes. Repair analysis by photolyase revealed inhibition of CPD repair at the edge of the TATA box in the active SNR6 promoter in vitro, but not in the GAL10 TATA box or in the inactive SNR6 promoter. Nucleotide excision repair was not inhibited, but preferentially repaired the 6-4PPs. We conclude that TBP can remain bound to damaged promoters and that nucleotide excision repair is the predominant pathway to remove UV damage in active TATA boxes.
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TATA-box binding protein promotes selective 6-4PP formation in the bent TATA box, while CPDs form preferentially at the TATA box edge and outside where DNA is not bent.
“One of the transcription factors, TATA-box binding protein (TBP), promotes the selective formation of 6-4PPs in the TATA-box, where the DNA is bent, but CPDs are formed preferentially at the edge of the TATA box and outside where the DNA is not bent [53].”
From Molecular Mechanisms of Ultraviolet Radiation‐Induced DNA Damage and Repair (2010) · cites this paper as [53]
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“One of the transcription factors, TATA-box binding protein (TBP), promotes the selective formation of 6-4PPs in the TATA-box, where the DNA is bent, but CPDs are formed preferentially at the edge of the TATA box and outside where the DNA is not bent [53].”
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- Authors
- Aboussekhra, A., & Thoma, F.
- Affiliations
- King Faisal Specialist Hospital & Research Centre (SA)
- ETH Zurich (CH)
- Corresponding author
- Thoma, Fritz
- Venue
- The EMBO Journal
- Published
- 1999-01-15
- Volume
- 18
- Issue
- 2
- Pages
- 433-443
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1171137
- OpenAlex
- W2159495010
- Cited by
- 47
- References
- 82
- Citations by year
- 2025: 2 · 2023: 2 · 2020: 1 · 2019: 1 · 2018: 4 · 2015: 1 · 2014: 4 · 2013: 2
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- TATA-binding protein, 6-4 photoproducts, UV-induced DNA damage, TATA box, nucleotide excision repair, photolyase, cyclobutane pyrimidine dimers, DNA repair, promoter accessibility, bent DNA, transcription initiation, GAL10, RNA polymerase II, RNA polymerase III, chromatin structure, yeast
- MeSH terms
- Base Sequence, DNA Damage, Deoxyribodipyrimidine Photo-Lyase, DNA Repair, DNA-Binding Proteins, DNA, Fungal, Genes, Fungal, Molecular Sequence Data, Photochemistry, Pyrimidine Dimers, Saccharomyces cerevisiae, Transcription Factors, Ultraviolet Rays, TATA Box, DNA Primers, TATA-Box Binding Protein
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