Spatial control of the GTPase MglA by localized RomR–RomX GEF and MglB GAP activities enables Myxococcus xanthus motility
| Autor: | Kristin Wuichet, Anna Potapova, Daniela Keilberg, Manon Wigbers, Lotte Søgaard-Andersen, Ulrich Gerland, Luis António Menezes Carreira, Andrea Harms, Dobromir Szadkowski |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Microbiology (medical)
Myxococcus xanthus GTPase-activating protein Polarity (physics) Gliding motility Immunology GTPase Applied Microbiology and Biotechnology Microbiology GTP Phosphohydrolases Nucleotide exchange factor 03 medical and health sciences Bacterial Proteins Genetics Guanine Nucleotide Exchange Factors Small GTPase 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry Molecular Motor Proteins GTPase-Activating Proteins Cell Polarity Cell Biology biology.organism_classification Cell biology Guanine nucleotide exchange factor Protein Binding |
| Zdroj: | Nature Microbiology. 4:1344-1355 |
| ISSN: | 2058-5276 |
| DOI: | 10.1038/s41564-019-0451-4 |
| Popis: | The rod-shaped Myxococcus xanthus cells move with defined front-rear polarity using polarized motility systems. A polarity module consisting of the small GTPase MglA, its cognate GTPase activating protein (GAP) MglB and RomR establishes this polarity. Agl-Glt gliding motility complexes assemble and disassemble at the leading and lagging pole, respectively. These processes are stimulated by MglA-GTP at the leading and MglB at the lagging pole. Here, we identify RomX as an integral component of the polarity module. RomX and RomR form a complex that has MglA guanine nucleotide exchange factor (GEF) activity and also binds MglA-GTP. In vivo RomR recruits RomX to the leading pole forming the RomR-RomX complex that stimulates MglA-GTP formation and binding, resulting in a high local concentration of MglA-GTP. The spatially separated and opposing activities of the RomR-RomX GEF at the leading and the MglB GAP at the lagging cell pole establish front-rear polarity by allowing the spatially separated assembly and disassembly of Agl-Glt motility complexes. Our findings uncover a regulatory system for bacterial cell polarity that incorporates a nucleotide exchange factor as well as an NTPase activating protein for regulation of a nucleotide-dependent molecular switch and demonstrate a spatial organization that is conserved in eukaryotes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink