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Nucleic Acids Research, 1992, Vol. 20, No. 15 3971-3976
© 1992

MOLECULAR BIOLOGY

In vitro replication of bacteriophage PRD1 DNA. Metal activation of protein-primed initiation and DNA elongation

Javier Caldentey, Luis Blanco1, Harri Savilahti, Dennis H. Bamford* and Margarita Salas1

Department of Genetics, University of Helsinki Arkadiankatu 7, 00100 Helsinki, Finland 1Centro de Biologia Molecular (CSIC-UAM), Universidad Autoònoma Canto Blanco, 28049 Madrid, Spain

*To whom Correspondence should be addressed

Received April 30, 1992. Revised July 2, 1992. Accepted July 2, 1992.

Bacteriophage PRD1 replicates its DNA by means of a protein-primed replication mechanism. Compared to Mg2+, the use of Mn2+ as the metal activator of the phage DNA polymerase results In a great stimulation of the initiation reaction. The molecular basis of the observed stimulatory effect is an Increase in the velocity of the reaction. The phage DNA polymerase Is also able to catalyze the formation of the initiation complex in the absence of DNA template. Although the presence of Mn2+ does not affect either the polymerization activity or the processlvity of the DNA polymerase, this metal is unable to activate the overall replication of the phage genome. This can be explained by a deletorious effect of Mn2+ on the 3'-5'-exonucleolytic andor the strand-displacement activity, the latter /being an intrinsic function of the viral DNA polymerase required for protein-primed DNA replication.


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