Charles M. Radding

Yale University

Election Year: 1995
Primary Section: 21, Biochemistry
Secondary Section: 26, Genetics
Membership Type: Emeritus

Research Interests

Homologous genetic recombination plays vital roles in the repair of DNA and in the segregation of chromosomes to progeny germ cells in higher organisms, including man. During segregation, recombination further shuffles the genetic deck, thus contributing to the uniqueness of each new individual. A bacterial protein we have been studying for more than 15 years, called RecA protein, lies at the heart of recombination. In a reaction initiated on single-stranded DNA in vitro, RecA protein forms a helical nucleoprotein filament that recognizes homology in duplex DNA. Using the energy of ATP, the helical filament then causes an exchange of strands that yields recombined DNA. The biological importance of these reactions is indicated by the universal distribution of proteins that are related to RecA protein and the evolutionary conservation of the helical nucleoprotein structure. Previous mechanistic studies of bacterial RecA protein are guiding current work on a human homolog. These studies, aimed at understanding recombination in man, have potential implications in gene targeting and gene therapy.

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