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PMID: 3060851 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Corrected and Republished Article

Potential role of proteolysis in the control of UvrABC incision.

Nucleic acids research ·Vol. 16 ·No. 22 ·1988-00-25 ·Pages 10903-12

Caron PR, Grossman L

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.

MeSH Terms
DNA Damage DNA Repair/radiation effects Endodeoxyribonucleases/metabolism Escherichia coli/enzymology,genetics Escherichia coli Proteins Kinetics Peptide Hydrolases/isolation & purification,metabolism Substrate Specificity Ultraviolet Rays
Chemicals
Escherichia coli Proteins Endodeoxyribonucleases endodeoxyribonuclease uvrABC Peptide Hydrolases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Caron P R
Department of Biochemistry, Johns Hopkins University, School of Hygiene and Public Health, Baltimore, MD 21205.
Grossman L
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1988-00-25
Pages
10903-12
Language
English
Region
England
NLM ID
0411011
PMCID
PMC338947
Subset
IM
Grants
NIGMS NIH HHS · 5ROI-GM22846 · United States
Corrections
RepublishedFrom
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