Superhelical stress restrained in plasmid DNA during repair synthesis initiated by the UvrA, B and C proteins in vitro.
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.
Backendorf
C
C
Department of Molecular Genetics, Gorlaeus Laboratories, Leiden University, The Netherlands.
Olsthoorn
R
R
van de Putte
P
P
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D004249:DNA Damage; D004265:DNA Helicases; D011088:DNA Ligases / Q000378:metabolism; D004256:DNA Polymerase I / Q000378:metabolism; D004260:DNA Repair; D004278:DNA, Superhelical / Q000378:metabolism*; D004706:Endodeoxyribonucleases / Q000378:metabolism; D004926:Escherichia coli / Q000032:analysis; D029968:Escherichia coli Proteins; D009690:Nucleic Acid Conformation; D010957:Plasmids; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D004278:DNA, Superhelical; D029968:Escherichia coli Proteins; C058093:UvrB protein, E coli; D004256:DNA Polymerase I; D004706:Endodeoxyribonucleases; C036385:endodeoxyribonuclease uvrABC; D000251:Adenosine Triphosphatases; C506746:UvrD protein, E coli; D004265:DNA Helicases; D011088:DNA Ligases