Characterization of a DNA binding protein of bacteriophage PRD1 involved in DNA replication. |
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| Authors: | T M Pakula J Caldentey M Serrano C Gutierrez J M Hermoso M Salas D H Bamford |
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| Affiliation: | Department of Genetics, University of Helsinki, Finland. |
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| Abstract: | Escherichia coli phage PRD1 protein P12, involved in PRD1 DNA replication in vivo, has been highly purified from E. coli cells harbouring a gene XII-containing plasmid. Protein P12 binds to single-stranded DNA as shown by gel retardation assays and nuclease protection experiments. Binding of protein P12 to single-stranded DNA increases about 14% the contour length of the DNA as revealed by electron microscopy. Binding to single-stranded DNA seems to be cooperative, and it is not sequence specific. Protein P12 also binds to double-stranded DNA although with an affinity 10 times lower than to single-stranded DNA. Using the in vitro phage phi 29 DNA replication system, it is shown that protein P12 stimulates the overall phi 29 DNA replication. |
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