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Nucleic Acids Research, 1988, Vol. 16, No. 20 9651-9662
© 1988

Articles

Involvement of a cryptic ATPase activity of UvrB and its proteolysis product, UvrB* in DNA repair

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.

The incision of damaged DNA by the Escherichia coli UvrABC endonuclease requires ATP hydrolysis. Although the deduced sequence of the UvtB protein suggests a putative ATP binding site, no nucleoside triphosphatase activity is demonstrable with the purified UvrB protein. The UvrB protein is specifically proteolyzed in E. coli cell extracts to yield a 70 kD fragment, referred to as UvrB*, which has been purified and is shown to possess a single-strand DNA dependent ATPase activity. Substrate specificity and kinetic analyses of UvrB* catalyzed nucleoode hydrolysis indicate that the stimulation in DNA dependent ATPase activity following formation of the UvrAB complex results from the activation of the normally sequestered UvrB associated ATPase. Using nucleotide analogues, it can be shown that this activity is essential to the DNA incision reaction carried out by the UvrABC complex.

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


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E. L. Hildebrand and L. Grossman
Introduction of a Tryptophan Reporter Group into the ATP Binding Motif of the Escherichia coli UvrB Protein for the Study of Nucleotide Binding and Conformational Dynamics
J. Biol. Chem., April 3, 1998; 273(14): 7818 - 7827.
[Abstract] [Full Text] [PDF]


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