Substrate range of the 40,000-Dalton DNA-photoreactivating enzyme from Escherichia coli
- 11 February 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (3) , 681-687
- https://doi.org/10.1021/bi00351a026
Abstract
We determined the ability of the 40,000-dalton Escherichia coli photoreactivating enzyme to act on a variety of pyrimidine-pyrimidine photoproduct substrates in nucleic acids. The enzyme is at least as active on cis-syn-cyclobutylpyrimidine dimers in supercoiled DNA as in linear DNA, but inactive on dimers in RNA. Both the phosphodiester bond internal to the deoxyriboses of the pyrimidines of the dimer and the N-glycosyl bond joining the pyrimidine to deoxyribose must be intact for enzyme action. The enzyme has no activity toward (6-4) pyrimidine-cytosine products in DNA.Keywords
This publication has 22 references indexed in Scilit:
- Cleavage of pyrimidine dimers in specific DNA sequences by a pyrimidine dimer DNA-glycosylase of M. luteusNature, 1980
- PYRIMIDINE DIMER FORMATION AND REPAIR IN HUMAN-SKIN1980
- A rapid DEAE disk assay for photoreactivation of pyrimidine dimers in [3H]DNAAnalytical Biochemistry, 1979
- DNA sequence at the integration sites of the insertion element IS1Cell, 1978
- DNA-REPAIR IN V-79 CELLS TREATED WITH COMBINATIONS OF UV-RADIATION AND N-ACETOXY-2-ACETYLAMINOFLUORENE1977
- Photomonomerization of pyrimidine dimers by indoles and proteinsJournal of Theoretical Biology, 1976
- Photosensitized splitting of thymine dimers in DNA by gene 32 protein from phage T 4Biochemical and Biophysical Research Communications, 1976
- The chemical nature of photoreactivable lesions in DNA.Proceedings of the National Academy of Sciences, 1965
- Pyrimidine dimers in UV-irradiated poly dI:dC.Proceedings of the National Academy of Sciences, 1965
- Nuclease-resistant sequences in ultraviolet-irradiated deoxyribonucleic acidBiochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, 1964