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Nucleic Acids Research, 1993, Vol. 21, No. 16 3725-3730
© 1993

MOLECULAR BIOLOGY

In Vitro replication of bacteriophage PRD1 DNA. Characterization of the protein-primed initiation site

Javier Caldentey1, Luis Blanco2, Dennis H. Bamford1,2 and Margarita Salas3

1Department of Genetics PO Box 17, 00014 University of Helsinki, Finaldn 2Institute of Biotechnology PO Box 17, 00014 University of Helsinki, Finaldn 3Centro de Biologia Molecular 'Severo Ochoa' (CSIC-UAM), Universidad Autonoma Canto Blanco, 28059 Madrid, Spain

Received May 5, 1993. Revised June 28, 1993. Accepted June 28, 1993.

Bacteriophage PRD1 replicates its DNA by means of a protein-primed replication mechanism. Using singlestranded oligonucleotide templates carrying the sequence corresponding to the 25 first bases of the 3é end of PRD1 DNA, and Mg2+ as the activating metal ion of the phage DNA polymerase, we show that the fourth base from the 3é end of the template directs, by base complementarity, the dNMP to be linked to the phage terminal protein (TP) in the initiation reaction. This result suggests that phage PRD1 maintains its 3é end DNA sequences via a sliding-back mechanism. The single-stranded DNA templates could not be replicated by the PRD1 DNA polymerase, much in contrast to the natural TP-DNA. Nevertheless, the analysis of the transition products obtained with TP-DNA and origin containing oligonucleotides suggests that sliding-back occurs stepwise, the fourth base being the directing position during the entire process.


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