Characterization of the phage π29 protein p5 as a single-stranded DNA binding protein. Function in π29 DNA-protein p3 replication

Abstract

The phage .vphi. 29 protein p5, required in vivo in the elongation step of .vphi. 29 DNA replication, was highly purified from Escherichia coli cells harbouring a gene 5-containing plasmid and from .vphi. 29-infected Bacillus subtilis. The protein was characterized as the gene 5 product by amino acid analysis and NH2-terminal sequence determination. The purified protein p5 was shown to bind to single-stranded DNA and to protect it against nuclease degradation. No effect of protein p5 was observed either on the formation of the p3-dAMP initiation complex or on the rate of elongation. However, protein p5 greatly stimulated .vphi. 29 DNA-protein p3 replication at incubation times where the replication in the absence of p5 leveled off.