Invitée équipe Y. Bourne: Shikha Ragav @AFMB -« Structural and functional analysis of FlhF, a multi-domain GTPase regulating flagella assembly in Pseudomonas aeruginosa »

Résumé

GTPases are hydrolases that act as timers or switches for various cellular processes. FlhF belongs to the SRP GTPases subfamily which includes proteins that are responsible for targeting of proteins to correct cellular destination. Like other SRP GTPases, FlhF comprises three distinct domains. Using X-ray crystallography, together with in vivo and in vitro approaches, we investigated the structural and functional features of FlhF and identified differences among FlhF proteins from flagellated bacteria.

Our results also suggest that different domains of FlhF work coherently to form a functional flagellum. We further show that FlhF GTPase activity is regulated through a mechanism that differs from the canonical regulatory mechanism described for SRP GTPases. These findings reveal distinctive features of FlhF-mediated flagellation in Pseudomonas aeruginosa and provide new insights into the mechanisms governing polar flagellar localization and assembly.