Characterization of a DNA binding protein of bacteriophage PRD1 involved in DNA replication.

AUTOR(ES)

Pakula, T M

RESUMO

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.

Documentos Relacionados

• In vitro replication of bacteriophage PRD1 DNA. Characterization of the protein-primed initiation site.
• In vitro replication of bacteriophage PRD1 DNA. Metal activation of protein-primed initiation and DNA elongation.
• The Small Viral Membrane-Associated Protein P32 Is Involved in Bacteriophage PRD1 DNA Entry
• Characterization of the DNA-protein complex at the termini of the bacteriophage PRD1 genome.
• Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.