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- W126565639 abstract "Recombination is a fundamental cellular process that operates continually to shape and reshape the genomes of all organisms and to promote repair of damaged DNA in times of stress. Long before any of the activities that drive recombination were identified, molecular models predicted intimate pairing of homologous chromosomes and a reciprocal exchange of single strands between the DNA molecules to form a heteroduplex intermediate that has become generally known as a Holliday junction. Subsequent processing of the junction intermediate into mature products coupled with repair of basepair mismatches in the heteroduplex DNA provided plausible explanations for the spectrum of recombinants normally observed in genetic crosses (Holliday 1964; Meselson and Radding 1975). More recent years have seen the discovery and characterisation of proteins that form, process, and resolve Holliday junctions. Most have been identified through the genetic and biochemical analysis of recombination activities in Escherichia coli, though some eukaryotic homologues are beginning to emerge. The RuvAB and RecG proteins reviewed here are novel types of DNA helicases that appear to act specifically to drive branch migration of Holliday intermediates. We have intentionally focused on the biological roles of these proteins. For a broader view of recombination in general and a more complete bibliography, we refer the reader to recent excellent reviews by West (1994), Clark and Sandier (1994), and Kowalczykowski et al. (1994)." @default.
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- W126565639 date "1995-01-01" @default.
- W126565639 modified "2023-10-13" @default.
- W126565639 title "The RuvAB and RecG Proteins of Escherichia coli" @default.
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- W126565639 doi "https://doi.org/10.1007/978-3-642-79488-9_4" @default.
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