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

Carole Gardiennet; Thomas Wiegand; Alexandre Bazin; Riccardo Cadalbert; Britta Kunert; Denis Lacabanne; Irina Gutsche; Laurent Terradot; Beat H Meier; Anja Böckmann

doi:10.1007/s10858-016-0018-0

Article dans une revue

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

Carole Gardiennet ^{1, 2} Thomas Wiegand ³ Alexandre Bazin ² Riccardo Cadalbert ³ Britta Kunert ² Denis Lacabanne ² Irina Gutsche ⁴ Laurent Terradot ² Beat H Meier ² Anja Böckmann ²

1 CRM2 - Cristallographie, Résonance Magnétique et Modélisations

2 MMSB - Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry

3 Physical Chemistry [ETH Zürich]

4 IBS - UMR 5075 - Institut de biologie structurale

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.

Keywords : Sediments Protein complexes Solid-state NMR DnaB DnaG Primosome Gardiennet Carole Wiegand Thomas Bazin Alexandre Cadalbert Riccardo Kunert Britta Lacabanne Denis Gutsche Irina Terradot Laurent Meier Beat H. Böckmann Anja

Type de document :

Article dans une revue

Domaine :

Sciences du Vivant [q-bio] / Biochimie, Biologie Moléculaire / Biologie structurale [q-bio.BM]

Liste complète des métadonnées

https://hal.univ-grenoble-alpes.fr/hal-01443306
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