Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease
| Autor: | D C Thomas, B Van Houten, Mahmoud Abdel-Monem, Aziz Sancar, Intisar Husain |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Adenosine Triphosphatases
Nuclease Endodeoxyribonucleases Multidisciplinary DNA Repair Models Genetic biology DNA polymerase DNA repair Oligonucleotide Escherichia coli Proteins DNA Helicases Helicase DNA Polymerase I Molecular biology Kinetics Biochemistry Escherichia coli biology.protein DNA polymerase I Research Article UvrABC endonuclease Nucleotide excision repair |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.82.20.6774 |
| Popis: | UvrABC excision nuclease (UvrA, UvrB, and UvrC proteins) of Escherichia coli removes nucleotide mono- and diadducts from DNA in the form of oligonucleotides 12 or 13 bases long. We find that the purified enzyme dissociates from DNA very slowly, if at all, in the absence of other proteins implicated in excision repair. Addition of DNA polymerase I and helicase II (UvrD protein) to the reaction mixture stimulates the turnover rate of the excision nuclease to a level comparable to that observed in vivo. |
| Databáze: | OpenAIRE |
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