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  • Title: Characterization of the Pf3 single-strand DNA binding protein by circular dichroism spectroscopy.
    Author: Powell MD, Gray DM.
    Journal: Biochemistry; 1993 Nov 23; 32(46):12538-47. PubMed ID: 8241145.
    Abstract:
    We have used circular dichroism (CD) spectroscopy and gel electrophoresis to characterize the single-strand DNA binding protein (ssDBP) of the bacteriophage Pf3 and its complexes with Pf3 DNA and various DNA and RNA homopolymers. The secondary structure of Pf3 ssDBP had < 1% alpha-helix and therefore was probably a beta-sheet structure like the fd gene 5 protein (g5p). From CD titrations, the binding stoichiometry of Pf3 ssDBP was two nucleotides per protein monomer (n = 2) for complexes formed with all of the nucleic acids except poly[r(U)], for which n = 3 (in a buffer of 10 mM Tris-HCl and 70 mM NaCl, pH 8.2). Evidence of an additional binding mode of n = 4 for complexes formed with Pf3 DNA was found by gel electrophoresis experiments. Pf3 ssDBP showed a marked sequence dependence in binding affinities similar to that known for the fd g5p.
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