DNA synthesis dependent on genetic recombination: characterization of a reaction catalyzed by purified bacteriophage T4 proteins.
To simulate a reaction that occurs in T4-infected cells, we have developed an in vitro DNA synthesis system that requires seven highly purified proteins encoded by this bacteriophage: the DNA polymerase "holoenzyme" (four proteins), gene 32 protein, dda DNA helicase, and uvsX protein - an enzyme that catalyzes homologous DNA pairing and is functionally homologous to the recA protein. In the reaction observed, the 3'OH end of one single-stranded DNA molecule primes DNA synthesis using a double-stranded DNA molecule of homologous sequence as the template. The uvsX protein continuously removes the new DNA chain from its template, so that DNA is synthesized by a conservative mechanism. This type of reaction, which requires the cooperation of recombination and replication enzymes, seems likely to be a general feature of DNA metabolism.
D000251:Adenosine Triphosphatases / Q000502:physiology; D004265:DNA Helicases / Q000502:physiology; D004261:DNA Replication; D004279:DNA, Viral / Q000096:biosynthesis; D004268:DNA-Binding Proteins / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology; D008957:Models, Genetic; D011938:Rec A Recombinases; D011995:Recombination, Genetic; D012689:Sequence Homology, Nucleic Acid; D013604:T-Phages / Q000235:genetics* / Q000502:physiology; D013698:Templates, Genetic; D014764:Viral Proteins / Q000502:physiology; D014779:Virus Replication
D004279:DNA, Viral; D004268:DNA-Binding Proteins; D008565:Membrane Proteins; C092863:UvsX protein, Enterobacteria phage T4; D014764:Viral Proteins; D011938:Rec A Recombinases; D000251:Adenosine Triphosphatases; D004265:DNA Helicases