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Nucleic Acids Research, 1980, Vol. 8, No. 22 5305-5316
© 1980

ENZYMOLOGY

Cleavage and circularization of single-stranded DNA: a novel enzymatic activity of {varphi}X174 A* protein

Shlomo Esienberg and Mitchell Finer{dagger}

Department of Biochemistry, Weizmann Institute of Science Rehovot, Israel

Received August 11, 1980.

Purified ØX gene A* protein cleaves ØX 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 bonding 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.

{dagger}Present address: Department of Biochemistry and Molecular Biology, Harvard University Cambridge, Mass. USA.


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