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PMID: 2987819 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Nucleic acids research ·Vol. 13 ·No. 4 ·1985-02-25 ·Pages 1239-49

Blanco L, Salas M

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.

MeSH Terms
Bacillus subtilis/genetics Bacteriophages/enzymology,genetics DNA Replication DNA, Single-Stranded/metabolism DNA-Directed DNA Polymerase/isolation & purification,metabolism Exonucleases/isolation & purification,metabolism Kinetics Substrate Specificity Viral Proteins/metabolism
Chemicals
DNA, Single-Stranded Viral Proteins DNA-Directed DNA Polymerase Exonucleases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Blanco L
Salas M
References (21)
21 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/13.4.1239
Published
1985-02-25
Pages
1239-49
Language
English
Region
England
NLM ID
0411011
PMCID
PMC341069
Subset
IM
Grants
NIGMS NIH HHS · 2 R01 GM27242-05 · United States
External Links
PubMed source DOI: 10.1093/nar/13.4.1239 PMC Full Text View journal details
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