Interaction between bacteriophage PM2 protein IV and DNA

R. Marcoli, Vincenzo Pirrotta, R. M. Franklin

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Abstract

The interaction between DNA and the structural protein IV of bacteriophage PM2 was studied by co-sedimentation, filter binding and electron microscopy. The co-sedimentation data and the sigmoid-shaped filter binding curve were interpreted in terms of co-operative binding. At a given DNA/protein input ratio, some DNA molecules were associated with a large amount of protein IV while others had no detectable protein bound to them. Electron microscopic examination of DNA-protein IV mixtures showed highly condensed DNA molecules alongside uncomplexed native DNA. Dissociation experiments revealed the presence of two types of complexes. Type I dissociated rapidly while type II had a long half-life. Dissociation of complexes obtained with increasing protein/DNA ratios suggested that the type I complex was a precursor of type II complex. Protein IV binds equally well to superhelical, relaxed or linear DNA as well as to single-stranded DNA. These observations lead to a model for the interaction and for the consequent alterations in the DNA structure.

Original languageEnglish (US)
Pages (from-to)107-131
Number of pages25
JournalJournal of molecular biology
Volume131
Issue number1
DOIs
StatePublished - Jun 15 1979
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • Molecular Biology

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