Escherichia coli RuvA and RuvB proteins involved in recombination repair: physical properties and interactions with DNA
| Autor: | Hideo Shinagawa, Atsuo Nakata, Hiroshi Iwasaki, Toshikazu Shiba |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
DNA
Bacterial DNA Repair DNA repair DNA Recombinant Biology medicine.disease_cause chemistry.chemical_compound Bacterial Proteins Tetramer Escherichia coli Genetics medicine Holliday junction Molecular Biology Adenosine Triphosphatases Recombination Genetic Escherichia coli Proteins DNA Helicases Branch migration DNA-Binding Proteins Solutions chemistry Biochemistry Chromatography Gel Electrophoresis Polyacrylamide Gel Protein quaternary structure Homologous recombination DNA |
| Zdroj: | Molecular and General Genetics MGG. 237:395-399 |
| ISSN: | 1432-1874 0026-8925 |
| Popis: | Escherichia coli RuvA and RuvB proteins are encoded by an SOS-regulated operon, which is involved in DNA repair and recombination. RuvB has weak ATPase activity, which is enhanced by the addition of RuvA and DNA, and RuvA and RuvB in the presence of ATP promote branch migration at Holliday junctions. In this work, the physical states of RuvA and RuvB and their interactions with DNA were studied by sedimentation analysis and gel filtration chromatography. RuvA formed a stable tetramer in solution, which resisted dissociation by SDS at room temperature. RuvB formed a dimer in solution. When RuvA and RuvB were mixed, an oligomer complex was formed consisting of a tetrameric form of RuvA and a dimeric form of RuvB, and this complex bound to DNA. The maximal enhancement of the RuvB ATPase activity by RuvA was achieved at this stoichiometry in the presence of excess DNA. |
| Databáze: | OpenAIRE |
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