The binding of an avian myetobiastosis virus bask 12,000 dalton protein to nucleic acids (original) (raw)

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,

Department of Chemistry and Biochemistry and School of Medicine, Southern Illinois University

Carbondale, IL 62901, USA

† Present address: Department of Pathology, University of Virginia Medical Center, Box 168, Charlottesville, VA 22901, USA.

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Department of Chemistry and Biochemistry and School of Medicine, Southern Illinois University

Carbondale, IL 62901, USA

Search for other works by this author on:

† Present address: Department of Pathology, University of Virginia Medical Center, Box 168, Charlottesville, VA 22901, USA.

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Published:

11 December 1979

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Beverly Jane Smitht, James M. Bailey, The binding of an avian myetobiastosis virus bask 12,000 dalton protein to nucleic acids, Nucleic Acids Research, Volume 7, Issue 7, 11 December 1979, Pages 2055–2072, https://doi.org/10.1093/nar/7.7.2055
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Abstract

The binding of a basic 12,000 dalton protein (pl2) from avian myeloblastosis virus to viral RNA and heterologous DNA has been investigated. The binding stoichiometries and constants were determined by an extrinsic fluorescence assay. In both cases each bound pl2 molecule occupies four nucleotides and the apparent binding constant is approximately 1 x 10 6 M −l . Binding is non-cooperative and there is no apparent difference in the interaction of pl2 with viral RNA or heterologous single-strand DNA. The relative binding constant at various ionic strengths was assayed by the nitrocellulose filter procedure. Analysis of the data revealed that each bound pl2 molecule forms three ion pairs with the nucleic acid.

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Author notes

† Present address: Department of Pathology, University of Virginia Medical Center, Box 168, Charlottesville, VA 22901, USA.

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