Substrate range of the 40,000-dalton DNA-photoreactivating enzyme from Escherichia coli.
Substrate range of the 40,000-dalton DNA-photoreactivating enzyme from Escherichia coli.
复制标题
来自大肠杆菌的 40,000 道尔顿 DNA 光复活酶的底物范围。
DOI:
10.1021/bi00351a026
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发表时间:
1986
期刊:
影响因子:
2.9
通讯作者:
Hanawalt,PC
中科院分区:
文献类型:
--
作者:
Sutherland,BM;Oliveira,OM;Ciarrocchi,G;Brash,DE;Haseltine,WA;Lewis,RJ;Hanawalt,PC
Roger J. Lewis1 and Philip C. Hanawalt Department of Biological Sciences, Stanford University, Stanford, California 94305 Received June 13, 1985 abstract: We determined the ability of the 40000-dalton Escherichia coli photoreactivating enzyme to act on a variety of pyrimidine-pyrimidinephotoproduct substrates in nucleic acids. The enzyme is at least as active on m-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-V-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.I^ iotoreactivating enzymes (photolyase, EC 4.1. 99.3) repair ultraviolet light (UV, 220-310 nm) 1 irradiated DNA by monomerizing c/s’-ijn-cyclobutylpyrimidine dimers (PD) in a light (300-600 nm)-dependent reaction (Setlow, J. K., et al., 1965; Setlow, R. B., et al., 1965). The apparent specificity of these enzymes (Setlow & Setlow, 1963) has allowed their