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PMID: 100608 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Genome-linked protein associated with the 5' termini of bacteriophage phi29 DNA.

Journal of virology ·Vol. 27 ·No. 3 ·1978-09-00 ·Pages 776-83

Yehle CO

Abstract

A DNA-protein complex was isolated from Bacillus subtilis bacteriophage phi29 by sucrose gradient sedimentation or gel filtration in the presence of agents known to break noncovalent bonds. A 28,000-dalton protein was released from this complex by subsequent hydrolysis of the DNA. The DNA-protein complex was examined for its susceptibility to enzymes which act upon the 5' and 3' termini of DNA molecules. It was susceptible to exonucleolytic degradation from the 3' termini by exonuclease III but not from the 5' termini by lambda exonuclease. Attempts to label radioactively the 5' termini by phosphorylation with T4 polynucleotide kinase were unsuccessful despite prior treatment with alkaline phosphatase or phosphatase treatment of denatured DNA. Removal of the majority of the bound protein by proteolytic digestion did not increase susceptibility. These results suggest that the linked protein is covalently attached to the 5' termini of phi29 DNA.

MeSH Terms
Bacillus subtilis Bacteriophages/analysis,metabolism DNA, Viral/analysis,metabolism Exonucleases/metabolism Peptide Hydrolases/metabolism Phosphorylation Polynucleotide 5'-Hydroxyl-Kinase/metabolism Protein Binding Viral Proteins/analysis,isolation & purification,metabolism
Chemicals
DNA, Viral Viral Proteins Polynucleotide 5'-Hydroxyl-Kinase Exonucleases Peptide Hydrolases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Yehle C O
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.27.3.776-783.1978
Published
1978-09-00
Pages
776-83
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC525865
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.27.3.776-783.1978 PMC Full Text View journal details
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