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PMID: 2499869 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Characterization of the phage phi 29 protein p5 as a single-stranded DNA binding protein. Function in phi 29 DNA-protein p3 replication.

Nucleic acids research ·Vol. 17 ·No. 10 ·1989-05-25 ·Pages 3663-72

Martín G, Lázaro JM, Méndez E, Salas M

Abstract

The phage phi 29 protein p5, required in vivo in the elongation step of phi 29 DNA replication, was highly purified from Escherichia coli cells harbouring a gene 5-containing plasmid and from phi 29-infected Bacillus subtilis. The protein was characterized as the gene 5 product by amino acid analysis and NH2-terminal sequence determination. The purified protein p5 was shown to bind to single-stranded DNA and to protect it against nuclease degradation. No effect of protein p5 was observed either on the formation of the p3-dAMP initiation complex or on the rate of elongation. However, protein p5 greatly stimulated phi 29 DNA-protein p3 replication at incubation times where the replication in the absence of p5 leveled off.

MeSH Terms
Amino Acids/analysis Bacillus subtilis/genetics,metabolism Bacteriophages/genetics,metabolism DNA Replication DNA, Viral/genetics DNA-Binding Proteins/genetics Escherichia coli/genetics Kinetics Plasmids Viral Proteins/genetics
Chemicals
Amino Acids DNA, Viral DNA-Binding Proteins Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Martín G
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Lázaro J M
Méndez E
Salas M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/17.10.3663
Published
1989-05-25
Pages
3663-72
Language
English
Region
England
NLM ID
0411011
PMCID
PMC317848
Subset
IM
Grants
NIGMS NIH HHS · 5 R01 GM27242-09 · United States
External Links
PubMed source DOI: 10.1093/nar/17.10.3663 PMC Full Text View journal details
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