Abstract |
Numerous DNA-interactive proteins have been shown to locate specific sequences within large domains of non-target DNA in vitro and in vivo by a one-dimensional diffusion mechanism; however, the biological significance of this process has not been evaluated. We have examined the biological consequences of sliding for the pyrimidine dimer-specific DNA repair enzyme T4 endonuclease V, an enzyme which scans non-target DNA both in vitro and in vivo. An endonuclease V mutant was constructed whose only altered biochemical characteristic, measured in vitro, was a loss in its ability to slide on non-target DNA. In contrast to the native enzyme, when the mutated endonuclease V was expressed in DNA repair-deficient Escherichia coli, no enhanced ultraviolet survival was conferred. These results suggest that the mechanisms which DNA-interactive proteins employ to enhance the probability of locating their target sequences are of significant biological importance.
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Authors | D R Dowd, R S Lloyd |
Journal | Journal of molecular biology
(J Mol Biol)
Vol. 208
Issue 4
Pg. 701-7
(Aug 20 1989)
ISSN: 0022-2836 [Print] Netherlands |
PMID | 2681789
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- DNA, Bacterial
- Pyrimidines
- Endodeoxyribonucleases
- deoxyribonuclease V
- pyrimidine
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Topics |
- DNA Repair
- DNA, Bacterial
(metabolism)
- Endodeoxyribonucleases
(metabolism)
- Escherichia coli
- Mutation
- Pyrimidines
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