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PMID: 3124105 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Interaction of the bacteriophage phi 29 protein p6 with double-stranded DNA.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 2 ·1988-01-00 ·Pages 314-8

Prieto I, Serrano M, Lázaro JM, Salas M, Hermoso JM

Abstract

The Bacillus subtilis bacteriophage phi 29 protein p6 binds to double-stranded DNA, but not to single-stranded DNA, as determined by a gel retardation assay. The nature of the interaction was further studied by DNase I "footprinting" experiments. Protein p6 binds to fragments containing the right or left terminal sequences of phi 29 DNA, producing a characteristic pattern of hypersensitive bands spaced about 24 nucleotides apart along most of the fragment, flanking protected regions. Binding of protein p6 to an internal phi 29 DNA fragment was also observed, but the footprint pattern was more salt sensitive than that obtained with the terminal phi 29 DNA fragments. By electron microscopy, protein p6 was shown to cover the DNA, totally or partially, from one end. In addition, binding of protein p6 to relaxed circular DNA induced positive supercoiling, indicating that a topological change in the DNA occurred.

MeSH Terms
Bacillus subtilis/metabolism Bacteriophages/metabolism Base Sequence DNA, Recombinant/metabolism DNA, Viral/genetics,metabolism Deoxyribonuclease I Molecular Sequence Data Plasmids Viral Proteins/metabolism
Chemicals
DNA, Recombinant DNA, Viral Viral Proteins Deoxyribonuclease I
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Prieto I
Centro de Biología Molecular, Universidad Autónoma de Madrid, Canto Blanco, Spain.
Serrano M
Lázaro J M
Salas M
Hermoso J M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.2.314
Published
1988-01-00
Pages
314-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC279538
Subset
IM
Grants
NIGMS NIH HHS · 5 R01 GM27242-07 · United States
External Links
PubMed source DOI: 10.1073/pnas.85.2.314 PMC Full Text View journal details
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