DNA synthesis dependent on genetic recombination: characterization of a reaction catalyzed by purified bacteriophage T4 proteins

Cell. 1986 Dec 5;47(5):793-806. doi: 10.1016/0092-8674(86)90522-2.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / physiology
  • DNA Helicases / physiology
  • DNA Replication*
  • DNA, Viral / biosynthesis
  • DNA-Binding Proteins / physiology
  • Membrane Proteins / physiology
  • Models, Genetic
  • Rec A Recombinases
  • Recombination, Genetic*
  • Sequence Homology, Nucleic Acid
  • T-Phages / genetics*
  • T-Phages / physiology
  • Templates, Genetic
  • Viral Proteins / physiology
  • Virus Replication


  • DNA, Viral
  • DNA-Binding Proteins
  • Membrane Proteins
  • UvsX protein, Enterobacteria phage T4
  • Viral Proteins
  • Rec A Recombinases
  • Adenosine Triphosphatases
  • DNA Helicases