FrzS acts as a polar beacon to recruit SgmX , a central activator of type IV pili during Myxococcus xanthus motility

Sarah Bautista (1) , Victoria Schmidt (2) , Annick Guiseppi (1) , Emillia M F Mauriello (1) , Bouchra Attia (2) , Latifa Elantak (2) , Tâm Mignot (1) , Romain Mercier (1)

1 LCB - Laboratoire de chimie bactérienne
2 LISM - Laboratoire d'ingénierie des systèmes macromoléculaires

In rod-shaped bacteria, type IV pili (Tfp) promote twitching motility by assembling and retracting at the cell pole. In Myxococcus xanthus, a bacterium that moves in highly coordinated cell groups, Tfp are activated by a polar activator protein, SgmX. However, while it is known that the Ras-like protein MglA is required for unipolar targeting, how SgmX accesses the cell pole to activate Tfp is unknown. Here, we demonstrate that a polar beacon protein, FrzS, recruits SgmX at the cell pole. We identified two main functional domains, including a Tfp-activating domain and a polarbinding domain. Within the latter, we show that the direct binding of MglA-GTP unveils a hidden motif that binds directly to the FrzS N-terminal response regulator (CheY). Structural analyses reveal that this binding occurs through a novel binding interface for response regulator domains. In conclusion, the findings unveil the protein interaction network leading to the spatial activation of Tfp at the cell pole. This tripartite system is at the root of complex collective behaviours in this predatory bacterium.

Mots clés: cell motility; CheY domain; Myxococcus xanthus; response regulator domain; type IV pili Subject Categories Cell Adhesion; Polarity & Cytoskeleton; Microbiology; Virology & Host Pathogen Interaction

Domaines: Sciences du Vivant [q-bio]

Sarah Bautista, Victoria Schmidt, Annick Guiseppi, Emillia M F Mauriello, Bouchra Attia, et al.. FrzS acts as a polar beacon to recruit SgmX , a central activator of type IV pili during Myxococcus xanthus motility. EMBO Journal, 2022, pp.e111661. ⟨10.15252/embj.2022111661⟩. ⟨hal-03855040⟩