TAILIEUCHUNG - Báo cáo Y học: The RuvABC resolvasome Quantitative analysis of RuvA and RuvC assembly on junction DNA

The RuvABC resolvasome ofEscherichia colicatalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. This process involves two key steps: branch migration, catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvAprotein, and resolution, which is catalysed by the RuvC endonuclease. | Eur. J. Biochem. 269 5492-5501 2002 FEBS 2002 doi The RuvABC resolvasome Quantitative analysis of RuvA and RuvC assembly on junction DNA Mark J. Dickman1 Stuart M. Ingleston2 Svetlana E. Sedelnikova3 John B. Rafferty3 Robert G. Lloyd2 Jane A. Grasby4 and David P. Hornby1 1Transgenomic Research Laboratory Krebs Institute Department of Molecular Biology and Biotechnology University of Sheffield UK Institute of Genetics University of Nottingham Queens Medical Centre UK 3Krebs Institute Department of Molecular Biology and Biotechnology University of Sheffield UK 4Krebs Institute Centre for Chemical Biology University of Sheffield UK The RuvABC resolvasome of Escherichia coli catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. This process involves two key steps branch migration catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein and resolution which is catalysed by the RuvC endonuclease. We have quantified the interaction of the RuvA protein with synthetic Holliday junctions and have shown that the binding of the protein is highly structure-specific and leads to the formation of a complex containing two tetramers of RuvA per Holliday junction. Our data are consistent with two tetramers of RuvA binding to the DNA recombination intermediate in a co-operative manner. Once formed this complex prevents the binding of RuvC to the Holliday junction. However the formation of a RuvAC complex can be observed following sequential addition of the RuvC and RuvA proteins. Moreover by examining the DNA recognition properties of a mutant RuvA protein E55R D56K we show that the charge on the central pin is critical for directing the structure-specific binding by RuvA. Keywords RuvABC resolvasome Hollidayjunction surface plasmon resonance. Genetic recombination is a fundamental cellular process that serves both to protect and expand the coding .

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