Deinococcus radiodurans UV endonuclease beta DNA incisions do not generate photoreversible thymine residues.
The ability of UV endonuclease beta of Deinococcus radiodurans to act as a pyrimidine dimer DNA glycosylase was investigated. Cell-free extracts of D. radiodurans exhibiting UV endonuclease beta activity failed to generate incisions in irradiated DNA that liberated free-thymine residues upon photoreversal with 254-nm light. This is in marked contrast to the pyrimidine dimer UV glycosylase of Micrococcus luteus that does liberate such residues. The result suggests that UV endonuclease beta incises DNA by true endonuclease action.
Evans
D M
DM
Department of Microbiology, Edinburgh University, Great Britain.
Moseley
B E
BE
D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism*; D045647:DNA Glycosylases; D045643:DNA Repair Enzymes; D004269:DNA, Bacterial / Q000378:metabolism / Q000528:radiation effects; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D008837:Micrococcus / Q000201:enzymology; D009699:N-Glycosyl Hydrolases / Q000378:metabolism; D011740:Pyrimidine Dimers / Q000378:metabolism*; D013941:Thymine / Q000032:analysis; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D011740:Pyrimidine Dimers; D004706:Endodeoxyribonucleases; C055508:UvsD protein, Deinococcus radiodurans; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D045643:DNA Repair Enzymes; D013941:Thymine