DOI: 10.1002/bies.950150108. Mechanism of action of the <i>Escherichia coli</i> UvrABC nuclease: Clues to the damage recognition problem

Mechanism of action of the Escherichia coli UvrABC nuclease: Clues to the damage recognition problem

10.1002/bies.950150108

Crossref journal-article

Wiley

BioEssays (311)

Abstract

AbstractDuring the process of E. coli nucleotide excision repair, DNA damage recognition and processing are achieved by the action of the uvrA, uvrB, and uvrC gene products. The availability of highly purified proteins has lead to a detailed molecular description of E. coli nucleotide excision repair that serves as a model for similar processes in eukaryotes. An interesting aspect of this repair system is the protein complex's ability to work on a vast array of DNA lesions that differ widely in their chemical composition and molecular architecture. Here we propose a model for damage recognition in which the UvrB protein serves as the component that confers enhanced specificity to a preincision complex. We hypothesize that one major determinant for the formation of a stable preincision complex appears to be the disruption of base stacking interactions by DNA lesions.

Bibliography

Van Houten, B., & Snowden, A. (1993). Mechanism of action of the Escherichia coli UvrABC nuclease: Clues to the damage recognition problem. BioEssays, 15(1), 51â59. Portico.

Authors 2

Ben Van Houten (first)
Amanda Snowden (additional)

References 49 Referenced 77

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10.1073/pnas.86.14.5237
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10.1093/nar/17.11.4145
10.1021/bi00232a009
10.1016/S0021-9258(18)99176-3 / J. Biol. Chem. / Both ATPase sites of Escherichia coli UvrA have functional roles in nucleotide excision repair by Thiagalingam S. (1991)
10.1021/bi00230a004
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10.1016/S0021-9258(18)99175-1 / J. Biol. Chem. / Deletion mutagenesis of the Escherichia coli UvrA protein localizes domains for DNA binding, damage recognition, and protein‐protein interactions by Claasen L. A. (1991)
10.1093/nar/16.20.9651
Seeley T. W. andGrossman L.(1989). Mutation in the Escherichia coli UvrB ATPase motif compromise repair capacity.Proc. Natl Acad. Sci. USA in press. (10.1073/pnas.86.17.6577)
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10.1016/0022-2836(91)90854-Y
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10.1073/pnas.88.4.1212
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10.1073/pnas.86.13.4833
10.1016/S0021-9258(18)66897-8 / J. Biol. Chem. / Activities and incision patterns of ABC excinuclease on modified DNA containing single‐base mismatches and extrahelical bases by Thomas D. C. (1986)
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10.1073/pnas.88.24.11574

Dates

Type	When
Created	20 years, 6 months ago (Feb. 25, 2005, 5:40 a.m.)
Deposited	1 year, 10 months ago (Oct. 24, 2023, 5:17 p.m.)
Indexed	4 weeks, 1 day ago (Aug. 6, 2025, 9:55 a.m.)
Issued	32 years, 8 months ago (Jan. 1, 1993)
Published	32 years, 8 months ago (Jan. 1, 1993)
Published Online	20 years, 6 months ago (Feb. 5, 2005)
Published Print	32 years, 8 months ago (Jan. 1, 1993)

Funders 0

None

BibTeX

@article{Van_Houten_1993, title={Mechanism of action of the Escherichia coli UvrABC nuclease: Clues to the damage recognition problem}, volume={15}, ISSN={1521-1878}, url={http://dx.doi.org/10.1002/bies.950150108}, DOI={10.1002/bies.950150108}, number={1}, journal={BioEssays}, publisher={Wiley}, author={Van Houten, Ben and Snowden, Amanda}, year={1993}, month=jan, pages={51–59} }

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