Specificity of the binding of bacteriophage M13 encoded gene-5 protein to DNA and RNA studied by means of fluorescence titrations.

Journal of Biomolecular Structure & Dynamics
H BulsinkC W Hilbers

Abstract

The fluorescence quenching of the bacteriophage M13 encoded gene-5 protein was used to study its binding characteristics to different polynucleotides. Experiments were performed at different salt concentrations and in some instances at different temperatures. The affinity of the protein depends on the base and sugar composition of the polynucleotides involved and may differ appreciably, i.e. by orders of magnitude. The salt dependence of binding is within experimental accuracy equal for all single stranded polynucleotides. A method is presented to estimate values of the cooperativity constant from salt titration curves. These values are systematically higher than those obtained from titration experiments in which protein is added to a polynucleotide solution. A comparison is made between the binding constants of the gene-5 protein and the gene-32 protein encoded by the T4 phage. Possible implications of the binding characteristics of the gene-5 protein for an understanding of its role in vivo are discussed.

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Citations

Jun 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·B Michel, N D Zinder
Sep 15, 1993·Proceedings of the National Academy of Sciences of the United States of America·W S Sandberg, T C Terwilliger
Jul 9, 1996·Proceedings of the National Academy of Sciences of the United States of America·X ChengR D Smith
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Dec 4, 2003·Biopolymers·Tung-Chung MouDonald M Gray
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Feb 20, 2002·Journal of Molecular Biology·Cathelijne P A M KloksCornelis W Hilbers
Feb 20, 1991·Journal of Molecular Biology·M L Carpenter, G G Kneale

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