ArticleThe EMBO journal2007
Coupling of protein localization and cell movements by a dynamically localized response regulator in Myxococcus xanthus.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 100 citations in OpenAlex.
- Structural and biophysical insights into RomR, MglB, and MglC interactions involved in regulating cell polarity in Myxococcus xanthus.The Journal of biological chemistry · 2025Article
- Combinatorial control of type IVa pili formation by the four polarized regulators MglA, SgmX, FrzS, and SopA.Journal of bacteriology · 2024Article
- A deterministic, c-di-GMP-dependent program ensures the generation of phenotypically similar, symmetric daughter cells during cytokinesis.Nature communications · 2024Article
- Molecular basis and design principles of switchable front-rear polarity and directional migration in Myxococcus xanthus.Nature communications · 2023Article
- Mathematical modeling of mechanosensitive reversal control inFrontiers in microbiology · 2023Article
- A bipartite, low-affinity roadblock domain-containing GAP complex regulates bacterial front-rear polarity.PLoS genetics · 2022Article
- Three PilZ Domain Proteins, PlpA, PixA, and PixB, Have Distinct Functions in Regulation of Motility and Development in Myxococcus xanthus.Journal of bacteriology · 2021Article
- The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Protein-protein interaction network controlling establishment and maintenance of switchable cell polarity.PLoS genetics · 2020Article
- Transcriptome dynamics of theeLife · 2019Article
- Spatial control of the GTPase MglA by localized RomR-RomX GEF and MglB GAP activities enables Myxococcus xanthus motility.Nature microbiology · 2019Article
- Evolutionary diversification of the RomR protein of the invasive deltaproteobacterium, Bdellovibrio bacteriovorus.Scientific reports · 2019Article
- A gated relaxation oscillator mediated by FrzX controls morphogenetic movements in Myxococcus xanthus.Nature microbiology · 2018Article
- Self-identity reprogrammed by a single residue switch in a cell surface receptor of a social bacterium.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- MglC, a Paralog of Myxococcus xanthus GTPase-Activating Protein MglB, Plays a Divergent Role in Motility Regulation.Journal of bacteriology · 2016Article
- Evolution and Design Governing Signal Precision and Amplification in a Bacterial Chemosensory Pathway.PLoS genetics · 2015Article
- Contact- and Protein Transfer-Dependent Stimulation of Assembly of the Gliding Motility Machinery in Myxococcus xanthus.PLoS genetics · 2015Article
- Evolution and diversity of the Ras superfamily of small GTPases in prokaryotes.Genome biology and evolution · 2014Article
- Dual biochemical oscillators may control cellular reversals in Myxococcus xanthus.Biophysical journal · 2014Article
- Cell division resets polarity and motility for the bacterium Myxococcus xanthus.Journal of bacteriology · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myxococcus xanthus cells harbor two motility machineries, type IV pili (Tfp) and the A-engine. During reversals, the two machineries switch polarity synchronously. We present a mechanism that synchronizes this polarity switching. We identify the required for motility response regulator (RomR) as essential for A-motility. RomR localizes in a bipolar, asymmetric pattern with a large cluster at the lagging cell pole. The large RomR cluster relocates to the new lagging pole in parallel with cell reversals. Dynamic RomR localization is essential for cell reversals, suggesting that RomR relocalization induces the polarity switching of the A-engine. The analysis of RomR mutants shows that the output domain targets RomR to the poles and the receiver domain is essential for dynamic localization. The small GTPase MglA establishes correct RomR polarity, and the Frz two-component system regulates dynamic RomR localization. FrzS localizes with Tfp at the leading pole and relocates in an Frz-dependent manner to the opposite pole during reversals; FrzS and RomR localize and oscillate independently. The Frz system synchronizes these oscillations and thus the synchronous polarity switching of the motility machineries.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.