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. 1972 Nov;69(11):3365–3369. doi: 10.1073/pnas.69.11.3365

Cleavage of Simian Virus 40 DNA at a Unique Site by a Bacterial Restriction Enzyme

John F Morrow 1, Paul Berg 1
PMCID: PMC389772  PMID: 4343967

Abstract

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.

Keywords: DNA mapping, adenovirus-SV40 hybrid, T4 gene 32 protein, electron microscopy, double-strand cleavage

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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