Chaperone Recycling in Late-Stage Flagellar Assembly

Rossi, Paolo; Xing, Qiong; Bini, Elisabetta; Portaliou, Athina G; Clay, Mary C.; Warren, Eric M.; Khanra, Nandish; Economou, Anastassios; Kalodimos, C.G.

doi:10.1016/j.jmb.2023.167954

Cited by 5 publications

(3 citation statements)

References 41 publications

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“…Bacterial attachment to the surface is an essential initial step in biofilm formation, which is facilitated by flagella. It has been suggested that the flagellum is responsible for motility in Gram-negative bacteria [33]. The primary components of flagellar are the matrix, hook, and filaments.…”

Section: Analysis Of Genes Associated With Biofilm Formation Flagella...mentioning

confidence: 99%

Transcriptome Reveals Regulation of Quorum Sensing of Hafnia alvei H4 on the Coculture System of Hafnia alvei H4 and Pseudomonas fluorescens ATCC13525

Wang,

Li,

Zhang

et al. 2024

Foods

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In the food industry, foodborne spoilage bacteria often live in mixed species and attach to each other, leading to changes in spoilage characteristics. Quorum sensing (QS) has been reported to be a regulating mechanism for food spoiling by certain kinds of bacteria. Here, the contents of biofilm, extracellular polysaccharides, and biogenic amines in the coculture system of Hafnia alvei H4 and Pseudomonas fluorescens ATCC13525 were significantly reduced when the QS element of H. alvei H4 was deleted, confirming that QS of H. alvei H4 is involved in the dual-species interactions. Then, transcriptomics was used to explore the regulatory mechanism at the mRNA molecular level. The deletion of the QS element decreased the transcript levels of genes related to chemotaxis, flagellar assembly, and the two-component system pathway of H. alvei H4 in the coculture system. Furthermore, a total of 732 DEGs of P. fluorescens ATCC13525 were regulated in the dual species, which were primarily concerned with biofilm formation, ATP-binding cassette transporters, and amino acid metabolism. Taken together, the absence of the QS element of H. alvei H4 weakened the mutual cooperation of the two bacteria in the coculture system, making it a good target for managing infection with H. alvei and P. fluorescens.

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Section: Analysis Of Genes Associated With Biofilm Formation Flagella...mentioning

confidence: 99%

Transcriptome Reveals Regulation of Quorum Sensing of Hafnia alvei H4 on the Coculture System of Hafnia alvei H4 and Pseudomonas fluorescens ATCC13525

Wang,

Li,

Zhang

et al. 2024

Foods

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“…Secretion of flagellum components utilizes a specialized Type III secretion system that is an integral part of the flagellum basal body (Abrusci et al, 2013;Halte & Erhardt, 2021;Kuhlen et al, 2018Kuhlen et al, , 2020. Closely associated with the export apparatus, and essential for efficient secretion of substrates, are the flagellum ATPase FliI, its binding partner FliH and FliJ (Fraser et al, 2003;Gonzalez-Pedrajo et al, 2002;Imada et al, 2016;Lane et al, 2006;Minamino & MacNab, 2000;Minamino & Namba, 2008;Rossi et al, 2023).…”

mentioning

confidence: 99%

“…Both FlgN and FliT also bind the export apparatus component FliJ (Bange et al, 2010;Evans et al, 2006;Imada et al, 2010;Kinoshita et al, 2013Kinoshita et al, , 2016Minamino, Kinoshita, Hara, et al, 2012;Xing et al, 2018). Recently, it was demonstrated that FliJ in an unfolded state can simultaneously bind both FlgN and FliT via distinct internal sites (Rossi et al, 2023). Both FlgN and FliT are required for the secretion of low abundance substrates immediately prior to filament formation.…”

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confidence: 99%

Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone

Dhindwal,

Boniecki,

Moore

2024

Protein Science

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In bacterial flagellum biogenesis, secretion of the hook‐filament junction proteins FlgK and FlgL and completion of the flagellum requires the FlgN chaperone. Similarly, the related FliT chaperone is necessary for the secretion of the filament cap protein FliD and binds the flagellar export gate protein FlhA and the flagellum ATPase FliI. FlgN and FliT require FliJ for effective substrate secretion. In Helicobacter pylori, neither FlgN, FliT nor FliJ have been annotated. We demonstrate that the genome location of HP1120 is identical to that of flgN in other flagellated bacteria and that HP1120 is the homologue of Campylobacter jejuni FlgN. A modeled HP1120 structure contains three α‐helices and resembles the FliT chaperone, sharing a similar substrate‐binding pocket. Using pulldowns and thermophoresis, we show that both HP1120 and a HP1120Δ126‐144 deletion mutant bind to FlgK with nanomolar affinity, but not to the filament cap protein FliD, confirming that HP1120 is FlgN. Based on size‐exclusion chromatography and multi‐angle light scattering, H. pylori FlgN binds to FlgK with 1:1 stoichiometry. Overall structural similarities between FlgN and FliT suggest that substrate recognition on FlgN primarily involves an antiparallel coiled‐coil interface between the third helix of FlgN and the C‐terminal helix of the substrate. A FlgNΔ126‐144 N100A, Y103A, S111I triple mutant targeting this interface significantly impairs the binding of FlgK. Finally, we demonstrate that FlgNΔ126‐144, like FliT, binds with sub‐micromolar affinity to the flagellum ATPase FliI or its N‐terminal domain. Hence FlgN and FliT likely couple delivery of low‐abundance export substrates to the flagellum ATPase FliI.This article is protected by copyright. All rights reserved.

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Sinorhizobium fredii HH103 flgJ is a flagellar gene induced by genistein in a NodD1- and TtsI- dependent manner

Navarro-Gómez,

Alías-Villegas,

Jiménez-Guerrero

et al. 2024

Plant Soil

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Background and aims Sinorhizobium fredii HH103 is a broad host-range rhizobial strain able to induce the formation of nitrogen-fixing nodules in dozens of legumes, including soybean. S. fredii HH103 exhibits genistein-induced surface motility. The aim of this work has been to determine whether the flgJ gene, which is inducible by genistein and codes for a flagellar protein, is involved in this motility and is relevant for symbiosis with soybean. Methods We have generated two independent mutants in the flgJ gene of HH103 and analysed their phenotypes in motility, exopolysaccharide production, biofilm formation, soybean root colonization, symbiosis with soybean, and secretion of effector proteins. We have also further studied the regulation of the expression of flgJ. Results We show that the expression of flgJ is driven by a tts box previously not detected, which accounts for its induction by flavonoids and the NodD1 and TtsI transcriptional activators. Inactivation of flgJ led to severe impairments in bacterial motility (swimming and genistein-induced surface motility) as well as to a significant reduction in symbiotic performance with soybean when bacteria are not directly inoculated onto the seedling roots. However, the absence of a functional FlgJ protein did not affect the bacterial ability to colonize soybean roots. Conclusion The flgJ gene of S. fredii HH103 connects the nod regulon with the genistein-induced surface motility exhibited by this rhizobial strain.

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Chaperone Recycling in Late-Stage Flagellar Assembly

Cited by 5 publications

References 41 publications

Transcriptome Reveals Regulation of Quorum Sensing of Hafnia alvei H4 on the Coculture System of Hafnia alvei H4 and Pseudomonas fluorescens ATCC13525

Transcriptome Reveals Regulation of Quorum Sensing of Hafnia alvei H4 on the Coculture System of Hafnia alvei H4 and Pseudomonas fluorescens ATCC13525

Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone

Sinorhizobium fredii HH103 flgJ is a flagellar gene induced by genistein in a NodD1- and TtsI- dependent manner

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