ArticlePLoS biology2019
Allosteric regulation of a prokaryotic small Ras-like GTPase contributes to cell polarity oscillations in bacterial motility.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Cell polarity control by an unconventional G-protein complex in bacteria.Nature communications · 2026Article
- Structural and biophysical insights into RomR, MglB, and MglC interactions involved in regulating cell polarity in Myxococcus xanthus.The Journal of biological chemistry · 2025Article
- Accurate prediction of protein function using statistics-informed graph networks.Nature communications · 2024Article
- A molecular switch controls assembly of bacterial focal adhesions.Science advances · 2024Article
- Identification of the mutual gliding locus as a factor for gut colonization in non-native bee hosts using the ARTP mutagenesis.Microbiome · 2024Article
- The eukaryotic-like characteristics of small GTPase, roadblock and TRAPPC3 proteins from Asgard archaea.Communications biology · 2024Article
- Basal cognition: shifting the center of gravity (again).Animal cognition · 2023Article
- Molecular basis and design principles of switchable front-rear polarity and directional migration in Myxococcus xanthus.Nature communications · 2023Article
- A bipartite, low-affinity roadblock domain-containing GAP complex regulates bacterial front-rear polarity.PLoS genetics · 2022Article
- ThemSystems · 2021Article
- Linking single-cell decisions to collective behaviours in social bacteria.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- Protein-protein interaction network controlling establishment and maintenance of switchable cell polarity.PLoS genetics · 2020Article
- Structural characterization of Myxococcus xanthus MglC, a component of the polarity control system, and its interactions with its paralog MglB.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutual gliding motility A (MglA), a small Ras-like GTPase; Mutual gliding motility B (MglB), its GTPase activating protein (GAP); and Required for Motility Response Regulator (RomR), a protein that contains a response regulator receiver domain, are major components of a GTPase-dependent biochemical oscillator that drives cell polarity reversals in the bacterium Myxococcus xanthus. We report the crystal structure of a complex of M. xanthus MglA and MglB, which reveals that the C-terminal helix (Ct-helix) from one protomer of the dimeric MglB binds to a pocket distal to the active site of MglA. MglB increases the GTPase activity of MglA by reorientation of key catalytic residues of MglA (a GAP function) combined with allosteric regulation of nucleotide exchange by the Ct-helix (a guanine nucleotide exchange factor [GEF] function). The dual GAP-GEF activities of MglB accelerate the rate of GTP hydrolysis over multiple enzymatic cycles. Consistent with its GAP and GEF activities, MglB interacts with MglA bound to either GTP or GDP. The regulation is essential for cell polarity, because deletion of the Ct-helix causes bipolar localization of MglA, MglB, and RomR, thereby causing reversal defects in M. xanthus. A bioinformatics analysis reveals the presence of Ct-helix in homologues of MglB in other bacterial phyla, suggestive of the prevalence of the allosteric mechanism among other prokaryotic small Ras-like GTPases.
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