Ff gene 5 protein has a high binding affinity for single-stranded phosphorothioate DNA

Biochemistry
T C MouD M Gray

Abstract

The gene 5 protein (g5p) of Ff bacteriophages is a well-studied model ssDNA-binding protein that binds cooperatively to the Ff ssDNA genome and single-stranded polynucleotides. Its affinity, K omega (the intrinsic binding constant times a cooperativity factor), can differ by several orders of magnitude for ssDNAs of different nearest-neighbor base compositions [Mou, T. C., Gray, C. W., and Gray, D. M. (1999) Biophys. J. 76, 1537-1551]. We found that the DNA backbone can also dramatically affect the binding affinity. The K omega for binding phosphorothioate-modified S-d(A)(36) was >300-fold higher than for binding unmodified P-d(A)(36) at 0.2 M NaCl. CD titrations showed that g5p bound phosphorothioate-modified oligomers with the same stoichiometry as unmodified oligomers. The CD spectrum of S-d(A)(36) underwent the same qualitative change upon protein binding as did the spectrum of unmodified DNA, and the phosphorothioate-modified DNA appeared to bind in the normal g5p binding site. Oligomers of d(A)(36) with different proportions of phosphorothioate nucleotides had binding affinities and CD perturbations intermediate to those of the fully modified and unmodified sequences. The influence of phosphorothioation on binding affinit...Continue Reading

References

Jan 1, 1995·Methods in Enzymology·R W Woody
Apr 1, 1993·Journal of Biomolecular Structure & Dynamics·V P Antao, D M Gray

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Citations

Dec 4, 2003·Biopolymers·Tung-Chung MouDonald M Gray
Oct 30, 2014·Frontiers in Chemistry·Pedro M D Moreno, Ana P Pêgo
Dec 1, 2006·American Journal of Physiology. Cell Physiology·Wenzhi TanMarco Colombini
May 24, 2020·International Journal of Molecular Sciences·Steven Ascoët, Michel De Waard

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