Ordered Conformational Changes in Damaged DNA Induced by Nucleotide Excision Repair Factors*
| Autor: | Jérôme Auriol, Jacqueline H. Enzlin, Diane Forget, Frédéric Coin, Jean-Marc Egly, Angels Tapias, Benoit Coulombe, Orlando D. Schärer |
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| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
DNA Repair
DNA repair DNA damage Biology Biochemistry Article chemistry.chemical_compound Transcription Factors TFII Adenosine Triphosphate Replication Protein A Humans Molecular Biology Replication protein A Nuclear Proteins Cell Biology DNA Endonucleases Molecular biology Cell biology Xeroderma Pigmentosum Group A Protein DNA-Binding Proteins Transcription Factor TFIIH DNA Repair Enzymes chemistry Transcription factor II H Nucleic Acid Conformation ERCC1 Nucleotide excision repair DNA Damage Transcription Factors |
| Popis: | In response to genotoxic attacks, cells activate sophisticated DNA repair pathways such as nucleotide excision repair (NER), which consists of damage removal via dual incision and DNA resynthesis. Using permanganate footprinting as well as highly purified factors, we show that NER is a dynamic process that takes place in a number of successive steps during which the DNA is remodeled around the lesion in response to the various NER factors. XPC/HR23B first recognizes the damaged structure and initiates the opening of the helix from position −3 to +6. TFIIH is then recruited and, in the presence of ATP, extends the opening from position −6 to +6; it also displaces XPC downstream from the lesion, thereby providing the topological structure for recruiting XPA and RPA, which will enlarge the opening. Once targeted by XPG, the damaged DNA is further melted from position −19 to +8. XPG and XPF/ERCC1 endo-nucleases then cut the damaged DNA at the limit of the opened structure that was previously “labeled” by the positioning of XPC/HR23B and TFIIH. |
| Databáze: | OpenAIRE |
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