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：11
页码：3365-3369
DOI：10.1073/pnas.69.11.3365
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The R1 restriction endonuclease of Escherichia coli converts covalently-closed circular Simian Virus 40 (SV40) DNA to unit-length linear duplex molecules. Cleavage occurs at a unique site, since denaturation and renaturation of these linear molecules yield linear but no circular molecules. The distance from the cleavage site to the SV40 DNA sequence contained in the adenovirus-SV40 hybrid, Ad2+ND1, is 0.11 of the length of SV40 DNA. T4 gene 32 protein binds to SV40 DNA in a region 0.45 of the length of SV40 DNA from the R1 cleavage site. E. coli B restriction endonuclease can cleave SV40 DNA at several sites.
关键词：DNA mapping ; adenovirus-SV40 hybrid ; T4 gene 32 protein ; electron microscopy ; double-strand cleavage
