DNA synthesis dependent on genetic recombination: characterization of a reaction catalyzed by purified bacteriophage T4 proteins.
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.
Polymerases:
Topics:
Accessory Proteins/Complexes, Nucleotide Incorporation, Enzyme Substrate Interactions
One line summary:
Seven T4 proteins (holoenzyme plus gp32, dda DNA helicase, and uvsX) in vitro to mimic a reaction in T4-infected cells involving recombination and replication enzymes.
Status:
| new | topics/pols set | partial results | complete | validated |
Results:
No results available for this paper.