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

Nucleic Acids Res. 1990 Nov 25;18(22):6553-7. doi: 10.1093/nar/18.22.6553.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Coliphages / drug effects
  • Coliphages / metabolism*
  • DNA / metabolism
  • DNA Replication / drug effects*
  • DNA, Single-Stranded / metabolism
  • DNA, Viral / biosynthesis*
  • DNA-Binding Proteins / genetics*
  • Nucleic Acid Conformation
  • Protein Conformation
  • Viral Proteins / pharmacology*

Substances

  • DNA, Single-Stranded
  • DNA, Viral
  • DNA-Binding Proteins
  • Viral Proteins
  • DNA