On the role of recA gene product in genetic recombination: an analysis by in vitro packaging of recombinant DNA molecules formed in the absence of protein synthesis.

The role of the recA gene product of Escherichia coli in genetic recombination was examined in a system where recombination takes place in the absence of protein synthesis. recA200 bacteria were infected with two mutant strains of phage lambda in the presence of chloramphenicol and rifampin, and the resulting recombinant DNA molecules were measured by in vitro packaging. When recA200 bacteria grown at a temperature that is permissive for RecA phenotype were transferred to a temperature that is restrictive for RecAa phenotype in the presence of the inhibitors, recombination of the infecting phages was severely blocked. This result shows that the recombination activity of the recA200 cells is inactivated by the change of temperature even in the absence of protein synthesis. The most likely explanation of this result is that the recA protein is directly involved in the recombination detected in the presence of chloramphenicol and rifampin.