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A molecular switch controls assembly of bacterial focal adhesions

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Attia, Bouchra | My, Laetitia | Castaing, Jean Philippe | Dinet, Céline | Le Guenno, Hugo | Schmidt, Victoria | Espinosa, Leon | Anantharaman, Vivek | Aravind, L. | Sebban-Kreuzer, Corinne | Nouailler, Matthieu | Bornet, Olivier | Viollier, Patrick | Elantak, Latifa | Mignot, Tâm

Edité par CCSD ; American Association for the Advancement of Science (AAAS) -

International audience. Cell motility universally relies on spatial regulation of focal adhesion complexes (FAs) connecting the substrate to cellular motors. In bacterial FAs, the Adventurous gliding motility machinery (Agl-Glt) assembles at the leading cell pole following a Mutual gliding-motility protein (MglA)–guanosine 5′-triphosphate (GTP) gradient along the cell axis. Here, we show that GltJ, a machinery membrane protein, contains cytosolic motifs binding MglA-GTP and AglZ and recruiting the MreB cytoskeleton to initiate movement toward the lagging cell pole. In addition, MglA-GTP binding triggers a conformational shift in an adjacent GltJ zinc-finger domain, facilitating MglB recruitment near the lagging pole. This prompts GTP hydrolysis by MglA, leading to complex disassembly. The GltJ switch thus serves as a sensor for the MglA-GTP gradient, controlling FA activity spatially.

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