Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.

Abstract : We here investigate the interactions between the DnaB helicase and the C-terminal domain of the corresponding DnaG primase of Helicobacter pylori using solid-state NMR. The difficult crystallization of this 387 kDa complex, where the two proteins interact in a six to three ratio, is circumvented by simple co-sedimentation of the two proteins directly into the MAS-NMR rotor. While the amount of information that can be extracted from such a large protein is still limited, we can assign a number of amino-acid residues experiencing significant chemical-shift perturbations upon helicase-primase complex formation. The location of these residues is used as a guide to model the interaction interface between the two proteins in the complex. Chemical-shift perturbations also reveal changes at the interaction interfaces of the hexameric HpDnaB assembly on HpDnaG binding. A structural model of the complex that explains the experimental findings is obtained.
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Article dans une revue
Journal of Biomolecular NMR, Springer Verlag, 2016, 64 (3), pp.189-95. 〈10.1007/s10858-016-0018-0〉
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Soumis le : lundi 23 janvier 2017 - 09:01:04
Dernière modification le : lundi 19 février 2018 - 14:34:03

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Carole Gardiennet, Thomas Wiegand, Alexandre Bazin, Riccardo Cadalbert, Britta Kunert, et al.. Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.. Journal of Biomolecular NMR, Springer Verlag, 2016, 64 (3), pp.189-95. 〈10.1007/s10858-016-0018-0〉. 〈hal-01443306〉

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