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PMID: 2931721 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 82 ·No. 20 ·1985-10-00 ·Pages 6774-8

Husain I, Van Houten B, Thomas DC, Abdel-Monem M, Sancar A

Abstract

UvrABC excision nuclease (UvrA, UvrB, and UvrC proteins) of Escherichia coli removes nucleotide mono- and diadducts from DNA in the form of oligonucleotides 12 or 13 bases long. We find that the purified enzyme dissociates from DNA very slowly, if at all, in the absence of other proteins implicated in excision repair. Addition of DNA polymerase I and helicase II (UvrD protein) to the reaction mixture stimulates the turnover rate of the excision nuclease to a level comparable to that observed in vivo.

MeSH Terms
Adenosine Triphosphatases/metabolism DNA Helicases DNA Polymerase I/metabolism DNA Repair Endodeoxyribonucleases/metabolism Escherichia coli/enzymology,genetics Escherichia coli Proteins Kinetics Models, Genetic
Chemicals
Escherichia coli Proteins DNA Polymerase I Endodeoxyribonucleases endodeoxyribonuclease uvrABC Adenosine Triphosphatases UvrD protein, E coli DNA Helicases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Husain I
Van Houten B
Thomas D C
Abdel-Monem M
Sancar A
References (27)
27 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.82.20.6774
Published
1985-10-00
Pages
6774-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC390769
Subset
IM
Grants
NIGMS NIH HHS · GM 32833 · United States
External Links
PubMed source DOI: 10.1073/pnas.82.20.6774 PMC Full Text View journal details
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