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Characterization of the phage ø29 protein p5 as a single-stranded DNA binding protein. Function in ø29 DNA-protein p3 replication

AuthorsMartín, Gil; Lázaro, José M. ; Méndez Cormán, Enrique; Salas, Margarita
Issue Date25-May-1989
PublisherOxford University Press
CitationNucleic Acids Research 36(10): 3409–341(2008)
AbstractThe phage π29 protein p5, required in vivo in the elongation step of π29 DNA replication, was highly purified from Escherichia coli cells harbouring a gene 5-containing plasmid and from π29-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 π29 DNA-protein p3 replication at incubation times where the replication in the absence of p5 leveled off.
Publisher version (URL)http://dx.doi.org/10.1093/nar/17.10.3663
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