Eukaryotic-like gephyrin and cognate membrane receptor coordinate corynebacterial cell division and polar elongation
Résumé
The order Corynebacteriales includes major industrial and pathogenic Actinobacteria such as Corynebacterium glutamicum or Mycobacterium tuberculosis. These bacteria have multi-layered cell walls composed of the mycolyl-arabinogalactan-peptidoglycan complex and a polar growth mode, thus requiring tight coordination between the septal divisome, organized around the tubulin-like protein FtsZ, and the polar elongasome, assembled around the coiled-coil protein Wag31. Here, using C. glutamicum, we report the discovery of two divisome members: a gephyrin-like r ep ur po sed m olyb do tr an sferase (Glp) and its membrane receptor (GlpR). Our results show how cell cycle progression requires interplay between Glp/GlpR, FtsZ and Wag31, showcasing a crucial crosstalk between the divisome and elongasome machineries that might be targeted for anti-mycobacterial drug discovery. Further, our work reveals that Corynebacteriales have evolved a protein scaffold to control cell division and morphogenesis, similar to the gephyrin/GlyR system that mediates synaptic signalling in higher eukaryotes through network organization of membrane receptors and the microtubule cytoskeleton. Cell division is central to bacterial physiology. Since the seminal work of Francois Jacob in 1968 on the filamentation temperature-sensitive (fts) genes in Escherichia coli, which led to the discovery of the tubulin-like bacterial cytoskeleton protein FtsZ 1 , a few well-studied model systems set the basis for our current knowledge of cell division at the molecular level. In this process, FtsZ regulates-through GTP-dependent polymerization-the assembly of the cell division machinery (the divisome) at the site of septation and governs the ordered assembly
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