Information essential for cell‐cycle‐dependent secretion of the 591‐residue <i>Caulobacter</i> hook protein is confined to a 21‐amino‐acid sequence near the <i>N‐</i>terminus

Kornacker, M. G.; Newton, Austin

doi:10.1111/j.1365-2958.1994.tb01268.x

Cited by 47 publications

(45 citation statements)

References 66 publications

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“…If FliE is exported, it should have regions of its sequence that constitute the recognition signal for its export by the flagellar apparatus. Other exported flagellar proteins (e.g., flagellin and hook protein) are recognized by N-terminal sequence (10,12). Consistent with this, FliE-V99G, with its mutation almost at the C terminus, was able to be exported, as judged by its ability to support the export of other substrates such as FlgD and to support motility, especially if overproduced and especially if in combination with the suppressor forms of FlgB.…”

Section: Flgb Is Probably the Most Proximal Of The Four Rod Proteinssupporting

confidence: 56%

Interaction between FliE and FlgB, a Proximal Rod Component of the Flagellar Basal Body of Salmonella

2000

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FliE is a flagellar basal body protein of Salmonella whose detailed location and function have not been established. A mutant allele of fliE, which caused extremely poor flagellation and swarming, generated extragenic suppressors, all of which mapped to flgB, one of four genes encoding the basal body rod; the fliE flgB pseudorevertants were better flagellated and swarmed better than the fliE parent, especially when the temperature was reduced from 37 to 30°C. Motility of the pseudorevertants in liquid culture was markedly better than motility on swarm plates; we interpret this to mean that reduced flagellation is less deleterious at low viscous loads. Overproduction of the mutant FliE protein improved the motility of the parental fliE mutant and its pseudorevertants, though not to wild-type levels. Overproduction of suppressor FlgB (but not wild-type FlgB) in the fliE mutant also resulted in improved motility. The second-site FlgB mutation by itself had no phenotype; cells swarmed as well as wild-type cells. When overproduced, wild-type FliE was dominant over FliE-V99G, but the reverse was not true; that is, overproduced FliE-V99G was not negatively dominant over wild-type FliE. We conclude that the mutant protein has reduced probability of assembly but, if assembled, functions relatively well. Export of the flagellar protein FlgD, which is known to be FliE dependent, was severely impaired by the FliE-V99G mutation but was significantly improved in the suppressor strains. The FliE mutation, V99G, was close to the C terminus of the 104-amino-acid sequence; the suppressing mutations in FlgB were all either G119E or G129D, close to the C terminus of its 138-amino-acid sequence. Affinity blotting experiments between FliE as probe and various basal body proteins as targets and vice versa revealed strong interactions between FliE and FlgB; much weaker interactions between FliE and other rod proteins were observed and probably derive from the known similarities among these proteins. We suggest that FliE subunits constitute a junction zone between the MS ring and the rod and also that the proximal rod structure consists of FlgB subunits.

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Section: Flgb Is Probably the Most Proximal Of The Four Rod Proteinssupporting

confidence: 56%

Interaction between FliE and FlgB, a Proximal Rod Component of the Flagellar Basal Body of Salmonella

2000

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“…In agreement with this idea, Kuwajima et al (25) have shown that 183 residues of the N terminus of the E. coli flagellin are required for secretion. Likewise, a 21-amino-acid sequence near the N terminus of a Caulobacter flagellar hook protein is essential for secretion of this protein via the flagellum-specific pathway (23). Possibly the C terminus contains the information needed to secrete FlaA from V. anguillarum.…”

Section: Discussionmentioning

confidence: 99%

Flagellin A is essential for the virulence of Vibrio anguillarum

et al. 1996

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A flagellin gene from the fish pathogen Vibrio anguillarum was cloned, sequenced, and mutagenized. The DNA sequence suggests that the flaA gene encodes a 40.1-kDa protein and is a single transcriptional unit. A polar mutation and four in-frame deletion mutations (180 bp deleted from the 5 end of the gene, 153 bp deleted from the 3 end of the gene, a double deletion of both the 180-and 153-bp deletions, and 942 bp deleted from the entire gene) were made. Compared with the wild type, all mutants were partially motile, and a shortening of the flagellum was seen by electron microscopy. Wild-type phenotypes were regained when the mutations were transcomplemented with the flaA gene. Protein analysis indicated that the flaA gene corresponds to a 40-kDa protein and that the flagellum consists of three additional flagellin proteins with molecular masses of 41, 42, and 45 kDa. N-terminal sequence analysis confirmed that the additional proteins were flagellins with N termini that are 82 to 88% identical to the N terminus of FlaA. Virulence studies showed that the N terminal deletion, the double deletion, and the 942-bp deletion increased the 50% lethal dose between 70-and 700-fold via immersion infection, whereas infection via intraperitoneal injection showed no loss in virulence. In contrast, the polar mutant and the carboxy-terminal deletion mutant showed approximately a 10 4 -fold increase in the 50% lethal dose by both immersion and intraperitoneal infection. In summary, FlaA is needed for crossing the fish integument and may play a role in virulence after invasion of the host.Vibrio anguillarum, which causes vibriosis in marine fish, is a highly pathogenic bacterium and has become a severe problem for the fish farming industry. An earlier study (3) has correlated the virulence of V. anguillarum with the possession of more than one flagellum. The importance of the flagellum as a potential virulence factor has been demonstrated for other bacteria. In Pseudomonas aeruginosa (5), three wild-type strains and their respective isogenic motility mutants were tested in the burned mouse model. The nonmotile mutants proliferated in the wound but did not cause the characteristic systemic infection, indicating that motility contributes to the invasive capabilities of this organism. For Campylobacter jejuni, the flagellum is the best-characterized virulence factor. In vitro studies using epithelial cell lines have shown that the flagellum aids the bacterium either in adherence to (30) or in internalization within (11) the cultured cells. A more recent study (47) shows that motility and not flagellin A is required for the invasion of intestinal cells by C. jejuni. However, flagellin A can serve as a secondary adhesin for the adherence to intestinal cells, whereas other adhesins are present to aid the motilitydependent internalization in an intestinal cell line. Similarly, for Vibrio cholerae, studies using spontaneous mutants or chemically derived motility mutants indicate that either motility (12) or an adhesin, proposed to be asso...

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“…In the flagellum, the N-terminal parts of the flagellin or hook protein have been identified as secretion signals, albeit the very N-termini were not strictly required for secretion [187][188][189]. Both the identified minimal export signal of the flagellin and fulllength anti-s 28 factor FlgM have been successfully used as export signals for substrates which could subsequently cleaved by TEV protease [190,191].…”

Section: Export Signalsmentioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

184

175

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One contribution of 12 to a theme issue 'The bacterial cell envelope'. The flagellum and the injectisome are two of the most complex and fascinating bacterial nanomachines. At their core, they share a type III secretion system (T3SS), a transmembrane export complex that forms the extracellular appendages, the flagellar filament and the injectisome needle. Recent advances, combining structural biology, cryo-electron tomography, molecular genetics, in vivo imaging, bioinformatics and biophysics, have greatly increased our understanding of the T3SS, especially the structure of its transmembrane and cytosolic components, the transcriptional, post-transcriptional and functional regulation and the remarkable adaptivity of the system. This review aims to integrate these new findings into our current knowledge of the evolution, function, regulation and dynamics of the T3SS, and to highlight commonalities and differences between the two systems, as well as their potential applications.

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Information essential for cell‐cycle‐dependent secretion of the 591‐residue Caulobacter hook protein is confined to a 21‐amino‐acid sequence near the N‐terminus

Cited by 47 publications

References 66 publications

Interaction between FliE and FlgB, a Proximal Rod Component of the Flagellar Basal Body of Salmonella

Interaction between FliE and FlgB, a Proximal Rod Component of the Flagellar Basal Body of Salmonella

Flagellin A is essential for the virulence of Vibrio anguillarum

Type III secretion systems: the bacterial flagellum and the injectisome

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