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Nucleic Acids Research, 1988, Vol. 16, No. 20 9641-9650
© 1988

Articles

Potential role of proteolysis in the control of UvrABC incision

Paul R. Caron+ and Lawrence Grossman

Department of Biochemistry, The Johns Hopkins University, School of Hygiene and Public Health 615 North Wolfe Street, Baltimore, MD 21205, USA

Received June 16, 1988. Accepted September 23, 1988.

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 UvtB* 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 protcin-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.

+Present address: Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA


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