Comparison of the cleavage of pyrimidine dimers by the bacteriophage T4 and Micrococcus luteus UV-specific endonucleases.
A comparison was made of the activity of the UV-specific endonucleases of bacteriophage T4 (T4 endonuclease V) and of Micrococcus luteus on ultravilet light-irradiated DNA substrates of defined sequence. The two enzymes cleave DNA at the site of pyrimidine dimers with the same frequency. The products of the cleavage reaction are the same, suggesting that the scission of DNA by T4 endonuclease V occurs via the combined actin of a pyrimidine dimer specific DNA glycosylase and an apyrimidinic-apurinic (AP) endonuclease as was recently shown for the M. luteus enzyme. The pyrimidine dimer DNA-glycosylase activity of both enzymes is more active on double-stranded DNA than it is on single-stranded DNA.
D001483:Base Sequence; D004247:DNA / Q000528:radiation effects*; D003851:Deoxyribonucleases / Q000378:metabolism*; D004720:Endonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D008837:Micrococcus / Q000201:enzymology*; D011740:Pyrimidine Dimers; D013604:T-Phages / Q000201:enzymology*; D014466:Ultraviolet Rays
D011740:Pyrimidine Dimers; D004247:DNA; D003851:Deoxyribonucleases; D004720:Endonucleases