Characterization of the phage phi 29 protein p5 as a single-stranded DNA binding protein. Function in phi 29 DNA-protein p3 replication.
The phage phi 29 protein p5, required in vivo in the elongation step of phi 29 DNA replication, was highly purified from Escherichia coli cells harbouring a gene 5-containing plasmid and from phi 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 phi 29 DNA-protein p3 replication at incubation times where the replication in the absence of p5 leveled off.
Martín
G
G
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Lázaro
J M
JM
Méndez
E
E
Salas
M
M
D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000235:genetics* / Q000378:metabolism; D001435:Bacteriophages / Q000235:genetics* / Q000378:metabolism; D004261:DNA Replication; D004279:DNA, Viral / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D007700:Kinetics; D010957:Plasmids; D014764:Viral Proteins / Q000235:genetics*
D000596:Amino Acids; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D014764:Viral Proteins