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. 1980 Nov 25;8(22):5305–5315. doi: 10.1093/nar/8.22.5305

Cleavage and circularization of single-stranded DNA: a novel enzymatic activity of phi X174 A* protein.

S Eisenberg, M Finer
PMCID: PMC324303  PMID: 6450942

Abstract

Purified phi X gene A* protein cleaves phi X single stranded DNA. The cleavage appears to be stoichiometric, whereby a gene A* protein molecule cleaves a phosphodiester bond and binds to the DNA fragment. The size of the cleavage product was inversely proportional to the ratio of A* protein to DNA in the reaction mixture. The cleavage of the DNA resulted in the formation of an A* protein - ssDNA complex identified on SDS-polyacrylamide gels and by banding in CsCl. An A* protein-ssDNA complex was isolated by gel filtration and shown to be active in a ligating reaction in which the two ends of the DNA fragment were joined to form a covalently closed circle. The joining reaction required Mg++ ions and was accompanied by the release of the protein from the DNA.

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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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