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PMID: 2525700 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

ATPase activity of the UvrA and UvrAB protein complexes of the Escherichia coli UvrABC endonuclease.

Nucleic acids research ·Vol. 17 ·No. 11 ·1989-06-12 ·Pages 4145-59

Oh EY, Claassen L, Thiagalingam S, Mazur S, Grossman L

Abstract

We have analyzed the ATPase activity exhibited by the UvrABC DNA repair complex. The UvrA protein is an ATPase whose lack of DNA dependence may be related to the ATP induced monomer-dimer transitions. ATP induced dimerization may be responsible for the enhanced DNA binding activity observed in the presence of ATP. Although the UvrA ATPase is not stimulated by dsDNA, such DNA can modulate the UvrA ATPase activity by decreases in Km and Vm and alterations in the Ki for ADP and ATP-gamma-S. The induction of such changes upon binding to DNA may be necessary for cooperative interactions of UvrA with UvrB that result in a DNA stimulated ATPase for the UvrAB protein complex. The UvrAB ATPase displays unique kinetic profiles that are dependent on the structure of the DNA effector. These kinetic changes correlate with changes in footprinting patterns, the stabilization of protein complexes on DNA damage and with the expression of helicase activity.

MeSH Terms
Adenosine Triphosphatases/genetics,metabolism Bacterial Proteins/genetics,metabolism DNA Repair DNA, Bacterial/metabolism Endodeoxyribonucleases/genetics,metabolism Escherichia coli/enzymology,genetics,metabolism Escherichia coli Proteins Kinetics Ultraviolet Rays
Chemicals
Bacterial Proteins DNA, Bacterial Escherichia coli Proteins Endodeoxyribonucleases endodeoxyribonuclease uvrABC Adenosine Triphosphatases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Oh E Y
Johns Hopkins University, Department of Biochemistry, Baltimore, MD 21205.
Claassen L
Thiagalingam S
Mazur S
Grossman L
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/17.11.4145
Published
1989-06-12
Pages
4145-59
Language
English
Region
England
NLM ID
0411011
PMCID
PMC317925
Subset
IM
Grants
NIGMS NIH HHS · R0I GM 22846 · United States
NIGMS NIH HHS · R0I GM 31110 · United States
External Links
PubMed source DOI: 10.1093/nar/17.11.4145 PMC Full Text View journal details
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