Characterization of a 3'----5' exonuclease activity in the phage phi 29-encoded DNA polymerase.
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.
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D001412:Bacillus subtilis / Q000235:genetics; D001435:Bacteriophages / Q000201:enzymology* / Q000235:genetics; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification / Q000378:metabolism*; D005092:Exonucleases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D013379:Substrate Specificity; D014764:Viral Proteins / Q000378:metabolism
D004277:DNA, Single-Stranded; D014764:Viral Proteins; D004259:DNA-Directed DNA Polymerase; D005092:Exonucleases