Interaction between DNA and Escherichia coli protein ω. Formation of a complex between single-stranded DNA and ω protein

R. E. Depew, Leroy-Fong Liu, J. C. Wang

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Abstract

Escherichia coli ω protein is found to form a complex with single-stranded coliphage fd DNA. The complex is stable in buoyant CsCl or Cs2SO4 density gradients. Addition of Mg(II) to the concentrated salt solutions, however, leads to the dissociation of the complex, even in the presence of EDTA in molar excess over Mg(II). The dissociated ω retains its enzymatic activity; the DNA recovered from the dissociated complex is indistinguishable from the original DNA. Exposure of the complex to alkali results in the cleavage of the DNA. This cleavage generates a 3'-hydroxyl DNA terminus, and the ω protein is found linked to the 5'-terminus, presumably covalently. Pronase digestion of the complex results initially in the removal of approximately 30% of the protein. A significant fraction of the residual complex is still stable in concentrated salt solutions, and can be dissociated by Mg(II). Extensive digestion with pronase results in the removal of the protein and the cleavage of the DNA chain.

Original languageEnglish
Pages (from-to)511-518
Number of pages8
JournalJournal of Biological Chemistry
Volume253
Issue number2
Publication statusPublished - 1978
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

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