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An examination has been made into the nature of the nucleoprotein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease when acting on a pyrimidine dimer-containing fd RF-I DNA species. The complexes of proteins and DNA form in unique stages. The first stage of binding involves an ATP-stimulated interaction of the UvrA protein with duplex DNA containing pyrimidine dimer sites. The UvrB protein significantly stabilizes the UvrA-pyrimidine dimer containing DNA complex which, in turn, provides a foundation for the binding of UvrC to activate the UvrABC endonuclease. The binding of one molecule of UvrC to each UvrAB-damaged DNA complex is needed to catalyze incision in the vicinity of pyrimidine dimer sites. The UvrABC-DNA complex persists after the incision event suggesting that the lack of UvrABC turnover may be linked to other activities in the excision-repair pathway beyond the initial incision reaction.
A T Yeung, and
W B Mattes, and
L Grossman
August 1993,
The Journal of biological chemistry,
A T Yeung, and
W B Mattes, and
L Grossman
June 1990,
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A T Yeung, and
W B Mattes, and
L Grossman
June 1989,
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A T Yeung, and
W B Mattes, and
L Grossman
June 1987,
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A T Yeung, and
W B Mattes, and
L Grossman
February 1994,
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A T Yeung, and
W B Mattes, and
L Grossman
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Postepy biochemii,
A T Yeung, and
W B Mattes, and
L Grossman
August 1988,
Nucleic acids research,
A T Yeung, and
W B Mattes, and
L Grossman
April 1993,
The Journal of biological chemistry,
A T Yeung, and
W B Mattes, and
L Grossman
January 1990,
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A T Yeung, and
W B Mattes, and
L Grossman
November 1988,
Proceedings of the National Academy of Sciences of the United States of America,
