ArticleJournal of bacteriology2016
HubP, a Polar Landmark Protein, Regulates Flagellar Number by Assisting in the Proper Polar Localization of FlhG in Vibrio alginolyticus.
Article in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- The polar landscape of bacterial pathogens and predators.Current opinion in microbiology · 2026Review
- Where and how many: evolutionary diversification of a molecular switch regulating flagellar patterns.Journal of bacteriology · 2026Review
- Spatio-genetically coordinated TPR domain-containing proteins modulate c-di-GMP signaling in Vibrio vulnificus.PLoS pathogens · 2025Article
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- Polar confinement of a macromolecular machine by an SRP-type GTPase.Nature communications · 2024Article
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- TipN's involvement with centromere segregation in Caulobacter crescentus.bioRxiv : the preprint server for biology · 2023Article
- Transcriptome analysis of the hepatopancreas from theFrontiers in cellular and infection microbiology · 2023Article
- Function and Structure of FlaK, a Master Regulator of the Polar Flagellar Genes in MarineJournal of bacteriology · 2022Article
- GGDEF domain as spatial on-switch for a phosphodiesterase by interaction with landmark protein HubP.NPJ biofilms and microbiomes · 2022Article
- Analysis of HubP-dependent cell pole protein targeting in Vibrio cholerae uncovers novel motility regulators.PLoS genetics · 2022Article
- Role of the N- and C-terminal regions of FliF, the MS ring component inJournal of bacteriology · 2021Article
- Interdependent Polar Localization of FlhF and FlhG and Their Importance for Flagellum Formation ofFrontiers in microbiology · 2021Article
- Motility of Vibrio spp.: regulation and controlling strategies.Applied microbiology and biotechnology · 2020Review
- Assembly mechanism of a supramolecular MS-ring complex to initiate bacterial flagellar biogenesis inJournal of bacteriology · 2020Article
- Regulation of the Single Polar Flagellar Biogenesis.Biomolecules · 2020Review
- Single molecule super-resolution imaging of bacterial cell pole proteins with high-throughput quantitative analysis pipeline.Scientific reports · 2019Article
- The GGDEF Domain of the Phosphodiesterase PdeB inJournal of bacteriology · 2019Article
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The marine bacterium Vibrio alginolyticus has a single polar flagellum, the number of which is regulated positively by FlhF and negatively by FlhG. FlhF is intrinsically localized at the cell pole, whereas FlhG is localized there through putative interactions with the polar landmark protein HubP. Here we focused on the role of HubP in the regulation of flagellar number in V. alginolyticus Deletion of hubP increased the flagellar number and completely disrupted the polar localization of FlhG. It was thought that the flagellar number is determined primarily by the absolute amount of FlhF localized at the cell pole. Here we found that deletion of hubP increased the flagellar number although it did not increase the polar amount of FlhF. We also found that FlhG overproduction did not reduce the polar localization of FlhF. These results show that the absolute amount of FlhF is not always the determinant of flagellar number. We speculate that cytoplasmic FlhG works as a quantitative regulator, controlling the amount of FlhF localized at the pole, and HubP-anchored polar FlhG works as a qualitative regulator, directly inhibiting the activity of polar FlhF. This regulation by FlhF, FlhG, and HubP might contribute to achieving optimal flagellar biogenesis at the cell pole in V. alginolyticus IMPORTANCE: For regulation of the flagellar number in marine Vibrio, two proteins, FlhF and FlhG, work as positive and negative regulators, respectively. In this study, we found that the polar landmark protein HubP is involved in the regulation of flagellar biogenesis. Deletion of hubP increased the number of flagella without increasing the amount of pole-localizing FlhF, indicating that the number of flagella is not determined solely by the absolute amount of pole-localizing FlhF, which is inconsistent with the previous model. We propose that cytoplasmic FlhG and HubP-anchored polar FlhG negatively regulate flagellar formation through two independent schemes.
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