文章基本信息

标题：Uncoupling of the recBC ATPase from DNase by DNA Crosslinked with Psoralen
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作者：Alexander E. Karu ; Stuart Linn
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：10
页码：2855-2859
DOI：10.1073/pnas.69.10.2855
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Exonucleolytic cleavage of DNA by the recBC DNase is accompained by a DNA-dependent ATP hydrolysis that ceases when the DNA that has been digested to a limit. On the other hand, DNA that has been crosslinked by 4,5',8-trimethylpsoralen in the presence of 360-nm light remains an effective cofactor in the ATPase reaction, but is resistant to digestion by the enzyme. Psoralentreated DNA is degraded by pancreatic DNase, micrococcal nuclease, and Escherichia coli B restriction enzyme, but not by Neurospora crassa nuclease, suggesting that crosslinking did not grossly distort the duplex structure of the DNA. The psoralen-DNA is not a potent inhibitor, but competes with single-stranded DNA from bacteriophage fd for the recBC DNase to roughly the same extent as does normal duplex DNA. DNA treated with psoralen in the dark, exposed to 360-nm light in the absence of psoralen, or treated with the intercalating agents ethidium bromide, 9-aminoacridine, ICR-191, or actinomycin D, responds to the enzyme no differently from untreated DNA. However, DNA crosslinked with mitomycin C or nitrogen mustard behaves similarly to psoralen-treated DNA. The relationship of these findings to models for the function and control of the recBC ATPase and nuclease, and the advantages of psoralen as a DNA crosslinking agent, are discussed.
关键词：DNA-dependent ATPase ; DNA intercalating agents ; exonuclease V ; E. coli