PMID: 10672034Feb 15, 2000Paper

31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes

European Journal of Biochemistry
C CastagnéM Delepierre

Abstract

Complexes of the HMG box protein SRY with two duplexes of 8 and 14 base pairs have been studied by 31P NMR and complete assignment of all phosphorus signals of the bound DNA duplexes are presented. While for the free DNA, all 31P signals display limited spectral dispersion (< 0.8 p.p.m.) for the bound duplexes, 31P resonances are spread over 2 p.p.m. Based on the previously published 3D structure of hSRY-HMG, with the 8 mer it is demonstrated that the upfield shifted resonances correspond to the site of partial intercalation of an isoleucine side chain into the DNA. Moreover, the observation of significant difference in linewidths between the two duplexes allows to estimate lifetime of the complexes from 31P-31P 2D exchange experiments.

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Citations

Dec 17, 2005·Proceedings of the National Academy of Sciences of the United States of America·Joon-Hwa LeeFiona Jucker
Dec 25, 2003·Journal of Biomolecular Structure & Dynamics·Stéphane TeletcheaJirí Kozelka
Aug 11, 2006·Nucleosides, Nucleotides & Nucleic Acids·Cynthia M Dupureur
Dec 20, 2002·Nucleic Acids Research·Péter VárnaiBrigitte Hartmann
Mar 11, 2011·Journal of the Royal Society, Interface·S CampagneA Milon
Jul 30, 2009·Journal of the American Chemical Society·Young-Min KangJoon-Hwa Lee
Oct 9, 2009·Chemistry : a European Journal·Stéphane TéletchéaJirí Kozelka
Apr 21, 2009·The Journal of Physical Chemistry. B·Guillaume P H SantiniCatherine Hervé du Penhoat
Nov 8, 2001·Journal of the American Chemical Society·B Luy, J P Marino
Jul 13, 2006·Journal of the American Chemical Society·Brahim HeddiBrigitte Hartmann

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