Characterization of a 3'----5' exonuclease activity in the phage phi 29-encoded DNA polymerase

Nucleic Acids Res. 1985 Feb 25;13(4):1239-49. doi: 10.1093/nar/13.4.1239.

Abstract

Purified protein p2 of phage phi 29, characterized as a specific DNA polymerase involved in the initiation and elongation of phi 29 DNA replication, contains a 3'----5' exonuclease active on single-stranded DNA, but not on double-stranded DNA. No 5'----3' exonuclease activity was found. The 3'----5' exonuclease activity was shown to be associated with the DNA polymerase since 1) the two activities were heat-inactivated with identical kinetics and 2) both activities, present in purified protein p2, cosedimented in a glycerol gradient.

Publication types

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

MeSH terms

  • Bacillus subtilis / genetics
  • Bacteriophages / enzymology*
  • Bacteriophages / genetics
  • DNA Replication
  • DNA, Single-Stranded / metabolism
  • DNA-Directed DNA Polymerase / isolation & purification
  • DNA-Directed DNA Polymerase / metabolism*
  • Exonucleases / isolation & purification
  • Exonucleases / metabolism*
  • Kinetics
  • Substrate Specificity
  • Viral Proteins / metabolism

Substances

  • DNA, Single-Stranded
  • Viral Proteins
  • DNA-Directed DNA Polymerase
  • Exonucleases