- Surfing on protein waves: proteophoresis as a mechanism for bacterial genome partitioning doi link

Auteur(s): Walter J.-C., Dorignac J., Lorman V., Rech Jérôme, Bouet Jean-yves, Nollmann Marcelo, Palmeri J., Parmeggiani A., Geniet F.

(Article) Publié: Physical Review Letters, vol. 119 p.028101 (2017)
Texte intégral en Openaccess : arxiv

Ref HAL: hal-01493262_v1
Ref Arxiv: 1702.07372
DOI: 10.1103/PhysRevLett.119.028101
Ref. & Cit.: NASA ADS
Exporter : BibTex | endNote
6 citations

Efficient bacterial chromosome segregation typically requires the coordinated action of a three-component machinery, fueled by adenosine triphosphate, called the partition complex. We present a phenomenological model accounting for the dynamic activity of this system that is also relevant for the physics of catalytic particles in active environments. The model is obtained by coupling simple linear reaction-diffusion equations with a proteophoresis, or “volumetric” chemophoresis, force field that arises from protein-protein interactions and provides a physically viable mechanism for complex translocation. This minimal description captures most known experimental observations: dynamic oscillations of complex components, complex separation, and subsequent symmetrical positioning. The predictions of our model are in phenomenological agreement with and provide substantial insight into recent experiments. From a nonlinear physics view point, this system explores the active separation of matter at micrometric scales with a dynamical instability between static positioning and traveling wave regimes triggered by the dynamical spontaneous breaking of rotational symmetry.

Commentaires: 6 pages, 3 figures