YscU/FlhB of Yersinia pseudotuberculosis Harbors a C-terminal Type III Secretion Signal

Login, Frédéric H.; Wolf‐Watz, Hans

doi:10.1074/jbc.m114.633677

Cited by 9 publications

(9 citation statements)

References 53 publications

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“…Destabilized YscU mutants that displayed increased rate constants of dissociation also enable secretion of Yops at 30°C, a temperature at which the wild-type strain effectively displays no Yop secretion. In addition, we previously identified a C-terminal secretion signal in YscU CC (29). Taken together, these findings suggest that YscU CC dissociation and subsequent secretion enabled by autoproteolysis play an important role in regulating Yop secretion.…”

Section: Discussionmentioning

confidence: 66%

“…YscP Protects the Slow Processing Mutant P264A from Autocleavage-It has been shown previously that the dissociation of YscU C into the two polypeptides YscU CC and YscU CN is required for Yop secretion and that YscU CC is subsequently secreted into the culture supernatant (27,29). The secretion of YscU CC through the T3SS is facilitated by a C-terminal secretion sequence, and the non-secreting phenotype observed for yscP-null mutants is partially rescued by the secondary suppressor mutants YscU…”

Section: E332amentioning

confidence: 99%

“…Also, we have shown that the dissociation of YscU C is required for Yop effector secretion (28). It was subsequently found that YscU C contains a C-terminal secretion signal domain (29). The deletion of the last 15 residues of YscU triggered an increase in YscF secretion without affecting Yop secretion (29).…”

mentioning

confidence: 99%

“…It was subsequently found that YscU C contains a C-terminal secretion signal domain (29). The deletion of the last 15 residues of YscU triggered an increase in YscF secretion without affecting Yop secretion (29). Thus, like YscP, YscU is involved in the substrate specificity switch.…”

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confidence: 99%

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Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in the Yersinia Type III Secretion System

Rogne

Edgren

et al. 2017

Journal of Biological Chemistry

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Edited by Thomas Sö llnerMany pathogenic Gram-negative bacteria use the type III secretion system (T3SS) to deliver effector proteins into eukaryotic host cells. In Yersinia, the switch to secretion of effector proteins is induced first after intimate contact between the bacterium and its eukaryotic target cell has been established, and the T3SS proteins YscP and YscU play a central role in this process. Here we identify the molecular details of the YscP binding site on YscU by means of nuclear magnetic resonance (NMR) spectroscopy. The binding interface is centered on the C-terminal domain of YscU. Disrupting the YscU-YscP interaction by introducing point mutations at the interaction interface significantly reduced the secretion of effector proteins and HeLa cell cytotoxicity. Interestingly, the binding of YscP to the slowly selfcleaving YscU variant P264A conferred significant protection against autoproteolysis. The YscP-mediated inhibition of YscU autoproteolysis suggests that the cleavage event may act as a timing switch in the regulation of early versus late T3SS substrates. We also show that YscU C binds to the inner rod protein YscI with a dissociation constant (K d ) of 3.8 M and with 1:1 stoichiometry. The significant similarity among different members of the YscU, YscP, and YscI families suggests that the protein-protein interactions discussed in this study are also relevant for other T3SS-containing Gram-negative bacteria.

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Section: Discussionmentioning

confidence: 66%

Section: E332amentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in the Yersinia Type III Secretion System

Rogne

Edgren

et al. 2017

Journal of Biological Chemistry

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“…This study, for the first time, showed that FlhB is involved in regulating the flagellar synthesis of important flagellar proteins, and that it affects the secretion of other bacterial proteins in L. monocytogenes . The main function of FlhB in Yersinia pseudotuberculosis is to mediate the transport of T3SS effector molecules and mediate the transport of bacterial toxins into host cells ( Minamino and Macnab, 2000a ; Macnab, 2004 ; Barker and Samatey, 2012 ; Login and Wolf-Watz, 2015 ; McMurry et al, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression in Listeria monocytogenes

Cui

Wang

et al. 2018

Front. Microbiol.

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Listeria monocytogenes is a food-associated bacterium that is responsible for food-related illnesses worldwide. In the L. monocytogenes EGD-e genome, FlhB, FliM, and FliY (encoded by lmo0679, lmo0699, and lmo0700, respectively) are annotated as putative flagella biosynthesis factors, but their functions remain unknown. To explore whether FlhB, FliM, and FliY are involved in Listeria flagella synthesis, we constructed flhB, fliM, fliY, and other flagellar-related gene deletion mutants using a homologous recombination strategy. Then, we analyzed the motility, flagella synthesis, and protein expression of these mutant strains. Motility and flagella synthesis were completely abolished in the absence of flhB, fliM, or fliY. These impaired phenotypes were fully restored in the complemented strains CΔflhB, CΔfliM, and CΔfliY. The transcriptional levels of flagellar-related genes, including flaA, fliM, fliY, lmo0695, lmo0698, fliI, and fliS, were downregulated markedly in the absence of flhB, fliM, or fliY. Deletion of flhB resulted in the complete abolishment of FlaA expression, while it decreased FliM and FliY expression. The expression of FlaA was abolished completely in the absence of fliM or fliY. No significant changes were found in the expression of FlhF and two flagella synthesis regulatory factors, MogR and GmaR. We demonstrate for the first time that FlhB, FliM, and FliY not only mediate Listeria motility, but also are involved in regulating flagella synthesis. This study provides novel insights that increase our understanding of the roles played by FlhB, FliM, and FliY in the flagellar type III secretion system in L. monocytogenes.

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The role and molecular mechanism of flgK gene in biological properties, pathogenicity and virulence genes expression of Aeromonas hydrophila

Lu,

Xiong,

Wei

et al. 2024

International Journal of Biological Macromolecules

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YscU/FlhB of Yersinia pseudotuberculosis Harbors a C-terminal Type III Secretion Signal

Cited by 9 publications

References 53 publications

Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in the Yersinia Type III Secretion System

Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in the Yersinia Type III Secretion System

Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression in Listeria monocytogenes

The role and molecular mechanism of flgK gene in biological properties, pathogenicity and virulence genes expression of Aeromonas hydrophila

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