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A Bipartite, Low-affinity Roadblock Domain-containing GAP Complex Regulates Bacterial Front-rear Polarity

Overview
Journal PLoS Genet
Specialty Genetics
Date 2022 Sep 6
PMID 36067225
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Abstract

The Ras-like GTPase MglA is a key regulator of front-rear polarity in the rod-shaped Myxococcus xanthus cells. MglA-GTP localizes to the leading cell pole and stimulates assembly of the two machineries for type IV pili-dependent motility and gliding motility. MglA-GTP localization is spatially constrained by its cognate GEF, the RomR/RomX complex, and GAP, the MglB Roadblock-domain protein. Paradoxically, RomR/RomX and MglB localize similarly with low and high concentrations at the leading and lagging poles, respectively. Yet, GEF activity dominates at the leading and GAP activity at the lagging pole by unknown mechanisms. Here, we identify RomY and show that it stimulates MglB GAP activity. The MglB/RomY interaction is low affinity, restricting formation of the bipartite MglB/RomY GAP complex almost exclusively to the lagging pole with the high MglB concentration. Our data support a model wherein RomY, by forming a low-affinity complex with MglB, ensures that the high MglB/RomY GAP activity is confined to the lagging pole where it dominates and outcompetes the GEF activity of the RomR/RomX complex. Thereby, MglA-GTP localization is constrained to the leading pole establishing front-rear polarity.

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References
1.
Leonardy S, Miertzschke M, Bulyha I, Sperling E, Wittinghofer A, Sogaard-Andersen L . Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP. EMBO J. 2010; 29(14):2276-89. PMC: 2910265. DOI: 10.1038/emboj.2010.114. View

2.
Li W, Cowley A, Uludag M, Gur T, McWilliam H, Squizzato S . The EMBL-EBI bioinformatics web and programmatic tools framework. Nucleic Acids Res. 2015; 43(W1):W580-4. PMC: 4489272. DOI: 10.1093/nar/gkv279. View

3.
Galicia C, Lhospice S, Varela P, Trapani S, Zhang W, Navaza J . MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus. Nat Commun. 2019; 10(1):5300. PMC: 6876712. DOI: 10.1038/s41467-019-13274-3. View

4.
Schumacher D, Sogaard-Andersen L . Regulation of Cell Polarity in Motility and Cell Division in Myxococcus xanthus. Annu Rev Microbiol. 2017; 71:61-78. DOI: 10.1146/annurev-micro-102215-095415. View

5.
Shen K, Rogala K, Chou H, Huang R, Yu Z, Sabatini D . Cryo-EM Structure of the Human FLCN-FNIP2-Rag-Ragulator Complex. Cell. 2019; 179(6):1319-1329.e8. PMC: 7008705. DOI: 10.1016/j.cell.2019.10.036. View