Potential role of proteolysis in the control of UvrABC incision
- PMID: 3060851
- PMCID: PMC338947
- DOI: 10.1093/nar/16.22.10903
Potential role of proteolysis in the control of UvrABC incision
Abstract
UvrB is specifically proteolyzed in Escherichia coli cell extracts to UvrB*. UvrB* is capable of interacting with UvrA in an apparently similar manner to the UvrB, however UvrB* is defective in the DNA strand displacement activity normally displayed by UvrAB. Whereas the binding of UvrC to a UvrAB-DNA complex leads to DNA incision and persistence of a stable post-incision protein-DNA complex, the binding of UvrC to UvrAB* leads to dissociation of the protein complex and no DNA incision is seen. The factor which stimulates this proteolysis has been partially purified and its substrate specificity has been examined. The protease factor is induced by "stress" and is under control of the htpR gene. The potential role of this proteolysis in the regulation of levels of active repair enzymes in the cell is discussed.
Corrected and republished from
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Potential role of proteolysis in the control of UvrABC incision.Nucleic Acids Res. 1988 Oct 25;16(20):9641-50. doi: 10.1093/nar/16.20.9641. Nucleic Acids Res. 1988. Corrected and republished in: Nucleic Acids Res. 1988 Nov 25;16(22):10903-12. doi: 10.1093/nar/16.22.10903. PMID: 16617483 Free PMC article. Corrected and republished.
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