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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (Tn-seq)

ABSTRACT: How cellular checkpoints couple the orderly assembly of macromolecular machines with cell cycle progression is poorly understood. The alpha-proteobacterium Caulobacter crescentus assembles a single polar flagellum during each cell cycle. We discovered that expression of multiple flagellin transcripts is licensed by a translational checkpoint responsive to a dual input signal: a secretion-competent hook-basal-body (HBB) structure and a surge in the FlaF secretion chaperone during cytokinesis, instructed by the cell cycle circuitry. We find that the unorthodox FljJ flagellin, one of six flagellin paralogs, acts as checkpoint linchpin, binding both FlaF and the FlbT translational regulator. FljJ recruits FlbT to inhibit translation at the 5’ untranslated region in other flagellin transcripts before HBB assembly. Once FlaF is synthesized and stabilized, it directs FljJ secretion through the HBB, thereby separating FlbT from its co-activator and relieving translational inhibition. The FlbT/FlaF pair is wide-spread and functional properties are conserved in alpha-proteobacteria, including pathogens.

ORGANISM(S): Caulobacter vibrioides NA1000

PROVIDER: GSE153949 | GEO | 2020/10/27

REPOSITORIES: GEO

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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (RNA-seq)

Project description:How cellular checkpoints couple the orderly assembly of macromolecular machines with cell cycle progression is poorly understood. The alpha-proteobacterium Caulobacter crescentus assembles a single polar flagellum during each cell cycle. We discovered that expression of multiple flagellin transcripts is licensed by a translational checkpoint responsive to a dual input signal: a secretion-competent hook-basal-body (HBB) structure and a surge in the FlaF secretion chaperone during cytokinesis, instructed by the cell cycle circuitry. We find that the unorthodox FljJ flagellin, one of six flagellin paralogs, acts as checkpoint linchpin, binding both FlaF and the FlbT translational regulator. FljJ recruits FlbT to inhibit translation at the 5’ untranslated region in other flagellin transcripts before HBB assembly. Once FlaF is synthesized and stabilized, it directs FljJ secretion through the HBB, thereby separating FlbT from its co-activator and relieving translational inhibition. The FlbT/FlaF pair is wide-spread and functional properties are conserved in alpha-proteobacteria, including pathogens.

2020-10-27 | GSE153858 | GEO

An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation

Project description:An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation

| PRJNA644605 | ENA

An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (Tn-seq)

Project description:An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (Tn-seq)

| PRJNA644598 | ENA

An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (RNA-seq)

Project description:An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (RNA-seq)

| PRJNA644363 | ENA

Analysis of microRNA expression in murine BMDCs activated by flagellin

Project description:MicroRNAs (miRNAs) are small non-coding RNA molecules that regulate gene expression by either translational inhibition or mRNA degradation. However, the role of miRNAs in inflammation induced by flagellin (ligand of TLR5) has not been fully determined, Here, we identified differentially expressed miRNAs in murine bone marrow-derived dendritic cells (BMDCs) between flagellin (FliC) treatment and medium alone using miRNA microarray. And we further evaluated the role of miRNAs in inflammation induced by flagellin.

2021-11-13 | GSE188656 | GEO

Flagellin (FliC) phosphorylation affects Type 2 protease secretion and biofilm dispersal in Pseudomonas aeruginosa PAO1

Project description:Protein phosphorylation has a major role in controlling the life-cycle and infection stages of bacteria. Proteome-wide occurrence of S/T/Y phosphorylation has been reported for many prokaryotic systems. Previously, we reported the phosphoproteome of Pseudomonas aeruginosa and Pseudomonas putida. In this study, we show the role of S/T phosphorylation of one motility protein, FliC, in regulating multiple surface-associated phenomena of Pseudomonas aeruginosa PAO1. The absence of phosphorylation in the conserved T27 and S28 residues of flagellin FliC, interestingly, did not affect swimming motility, but affected the secretome of type 2 secretion system (T2SS) and biofilm formation of PAO1. Flagellin phosphomutants had increased levels and activities of type 2 secretome proteins. This occurs by a possible mechanism affecting the secretion efficiency of T2SS machinery. Flagellin phosphomutants also formed reduced biofilm at 24h and had delayed biofilm dispersal under static and dynamic flow conditions, respectively. The levels of type 2 secretome and biofilm formation under static conditions had an inverse correlation. Hence, increase in the levels of type 2 secretome was accompanied by reduced biofilm formation in the flagellin phosphomutants. Altogether, we found a system of phosphorylation that co-ordinately regulates surface related processes such as proteases secretion by T2SS, biofilm formation and dispersal.

2022-03-02 | PXD003645 | Pride

C. difficile strain 630 flagellin C modifications

Project description:In proteomics, the study of post-translational modifications often relies on some type of enrichment strategy. Here, we show that an approach that is commonly used in phosphoproteomics (Immobilised Metal Affinity Chromatography (Fe3+-IMAC)) also enriches for peptides with a unique post-translational modification, known as type A, in the human pathogen Clostridioides difficile. The type A modification consists of a monosaccharide (GlcNAc) that is linked to an N-methylated threonine through a phosphodiester bond. This structure has previously been described on flagellin C of several C. difficile strains and is important for bacterial motility. Using LC-MS/MS analyses of IMAC-captured tryptic peptides, we not only observed Type A modified C. difficile flagellin peptides but also a variety of truncated/modified Type A structures on these peptides. Using an elaborate set of mass spectrometry analyses, we demonstrate that one of these modifications consists of a Type A structure containing a phosphonate (2-aminoethylphosphonate, 2-AEP), a modification that is rarely observed and has hitherto not been described in C. difficile.

2022-04-04 | PXD029552 | Pride

Re-annotated role of beta-Galactosidase in Flagellin deglycosylation

Project description:Most Eukaryotes recognise flagellin as a signature of bacterial invasion. In contrast to animals, plants do not recognise flagellin proteins, but conserved peptides released from flagellin (Felix et al., 1999). However, these peptides (e.g. flg22) are folded and buried deeply inside the flagellin polymer and would need to be released before they can interact with cell surface receptors, such as FLS2 (Fliegman & Felix, 2016). Here we discovered that the hydrolytic pathway releasing the flagellin elicitor in plants is initiated by a host-secreted beta-galactosidase (BGAL), which removes the terminal modified viosamine (mVio) from the O-glycan that cloaks the flagellin polymer. BGAL contributes to flagellin-dependent immunity but only against bacterial Pseudomonas syringae strains that carry mVio. Signatures of arms races at this new level of antagonistic interactions are that BGAL is suppressed during infection by a heat stable metabolite secreted by bacteria, and that other P. syringae strains carry BGAL-insensitive O-glycans.

2019-04-15 | PXD010461 | Pride

Pig-specific skin transcriptional responses after intradermal administration of flagellin

Project description:The study aimed at defining the skin innate responses after intradermal injection of flagellin. For this purpose, pigs were immunized by intradermal route with flagellin and H1N1 antigen. Skin was then sampled for microarray analyses.

2016-01-31 | GSE72256 | GEO

bak1bkk1 - Flagellin response in mpk mutants

Project description:au-09-01_mpk_flagellin_edu - bak1bkk1 - Investigate flagellin mpk dependent genes by comparision between bak1bkk1 and col-0. Keywords: gene knock out

2012-01-01 | GSE23185 | GEO

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