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PMID: 2557590 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Superhelical stress restrained in plasmid DNA during repair synthesis initiated by the UvrA, B and C proteins in vitro.

Nucleic acids research ·Vol. 17 ·No. 24 ·1989-12-25 ·Pages 10337-51

Backendorf C, Olsthoorn R, van de Putte P

Abstract

Purified UvrA, UvrB, UvrC, UvrD, PolA and Lig proteins from Escherichia coli have been used to assess the effect of nucleotide excision repair on the conformation of native negatively supercoiled plasmid DNA in an in vitro test system. The analysis of labeled reaction products on specific gel systems suggests that the Uvr excinuclease has the ability to restrain the superhelical stress in the template DNA during the repair process. This feature, observed in the case of the Uvr system is not found if the repair reaction is initiated by T4 endonuclease V or Micrococcus luteus UV endonuclease.

MeSH Terms
Adenosine Triphosphatases/metabolism Bacterial Proteins/metabolism DNA Damage DNA Helicases DNA Ligases/metabolism DNA Polymerase I/metabolism DNA Repair DNA, Superhelical/metabolism Endodeoxyribonucleases/metabolism Escherichia coli/analysis Escherichia coli Proteins Nucleic Acid Conformation Plasmids Ultraviolet Rays
Chemicals
Bacterial Proteins DNA, Superhelical Escherichia coli Proteins UvrB protein, E coli DNA Polymerase I Endodeoxyribonucleases endodeoxyribonuclease uvrABC Adenosine Triphosphatases UvrD protein, E coli DNA Helicases DNA Ligases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Backendorf C
Department of Molecular Genetics, Gorlaeus Laboratories, Leiden University, The Netherlands.
Olsthoorn R
van de Putte P
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/17.24.10337
Published
1989-12-25
Pages
10337-51
Language
English
Region
England
NLM ID
0411011
PMCID
PMC335304
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/17.24.10337 PMC Full Text View journal details
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