Nucleic Acids Research, 1989, Vol. 17, No. 10 3663-3672
© 1989
MOLECULAR BIOLOGY |
Characterization of the phage 
29 protein p5 as a single-stranded DNA binding protein. Function in 29 DNA-protein p3 replication
1Servicio de Endocnnologìa, Centro Ramòn y Cajal, Carretera de Colmenar Viejo Km 9.1. 28034 Madrid, Spain Centro de Biologia Molecular (CSIC-UAM). Universidad Autònoma Canto Blanco, 28049 Madrid
Received March 3, 1989. Revised April 18, 1989. Accepted April 18, 1989.
The phage 
29 protein p5, required in vivo in the elongation step of 29 DNA replication, was highly purified from Escherichia coli cells harbouring a gene 5-containing plasmid and from 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 29 DNA-protein p3 replication at incubation times where the replication in the absence of p5 leveled off.
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