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Nucleic Acids Research, 1981, Vol. 9, No. 9 2037-2054
© 1981

MOLECULAR BIOLOGY

Enzymatic properties of the bacteriophage {varphi}X174 A* protein on superhelical {varphi}X174 DNA: a model for the termination of the rolling circle DNA replication

A. van der Ende1, S.A. Langeveld1, R. Teertstra2, G.A. van Arkel1,2 and P.J. Weisbeek1,2

1Institute of Molecular Biology, State University of Utrecht Utrecht, The Netherlands 2Department of Molecular Cell Biology, State University of Utrecht Utrecht, The Netherlands

Received March 13, 1981. Incubation of {varphi}X174 replication form I DNA with the A* protein of {varphi}X174 in the presence of Mn2+ results in the formation of three different types of DNA molecules: open circular form DNA (RFII), linear form DNA (RFIII) and relaxed covalently closed form DNA (RFIV). The RFII and RFIII DNAs are shown to be A* protein-DNA complexes by electron microscopy using the protein labeling technique of Wu and Davidson (1). The linear double-stranded RFIII DNA molecule carries at one end a covalently attached A* protein whereas at the other end of the molecule the single-stranded termini are covalently linked to each other. The structure of the RFIII DNA shows its way of formation. The described properties of the A* protein indicate the way the larger A protein functions in the termination step of the rolling-circle type of {varphi}X174 DNA replication.


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