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

Authors
Journal
Cell
0092-8674
Publisher
Elsevier
Publication Date
Volume
47
Issue
5
Identifiers
DOI: 10.1016/0092-8674(86)90522-2
Disciplines
  • Biology

Abstract

Abstract 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.

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