Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori. - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue Journal of Biomolecular NMR Année : 2016

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

Irina Gutsche

Résumé

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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Dates et versions

hal-01443306 , version 1 (24-11-2020)

Identifiants

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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, 2016, 64 (3), pp.189-95. ⟨10.1007/s10858-016-0018-0⟩. ⟨hal-01443306⟩
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