Molecular and functional analysis of the type III secretion signal of the <i>Salmonella enterica</i> InvJ protein

Rüssmann, Holger; Kubori, Tomoko; Sauer, Jeannette; Galán, Jorge E.

doi:10.1046/j.1365-2958.2002.03196.x

Cited by 77 publications

(82 citation statements)

References 33 publications

(51 reference statements)

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“…Similar results have also been reported for the secretion signal consisting of the first 28 codons of a plant effector protein from Xanthomonas campestris (AvrBs2) and the secretion signal consisting of codons 4 to 7 of a secretion substrate from Salmonella enterica (InvJ) (24,30). Further, synonymous substitutions of codons, which change the sequence of the mRNA but leave the amino acid sequence intact, render the minimal secretion signal of yopQ or yopN nonfunctional (27,28).…”

supporting

confidence: 80%

A Synonymous Mutation in Yersinia enterocolitica yopE Affects the Function of the YopE Type III Secretion Signal

Ramamurthi

Schneewind

2005

J Bacteriol

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Yersinia spp. inject virulence proteins called Yops into the cytosol of target eukaryotic cells in an effort to evade phagocytic killing via a dedicated protein-sorting pathway termed type III secretion. Previous studies have proposed that, unlike other protein translocation mechanisms, Yops are not recognized as substrates for secretion via a solely proteinaceous signal. Rather, at least some of this information may be encoded within yop mRNA. Herein, we report that the first seven codons of yopE, when fused to the reporter protein neomycin phosphotransferase (Npt), are sufficient for the secretion of YopE 1-7 -Npt when type III secretion is induced in vitro. Systematic mutagenesis of yopE codons 1 to 7 reveals that, like yopQ, codons 2, 3, 5, and 7 are sensitive to mutagenesis, thereby defining the first empirical similarity between the secretion signals of two type III secreted substrates. Like that of yopQ, the secretion signal of yopE exhibits a bipartite nature. This is manifested by the ability of codons 8 to 15 to suppress point mutations in the minimal secretion signal that change the amino acid specificities of particular codons or that induce alterations in the reading frame. Further, we have identified a single nucleotide position in codon 3 that, when mutated, conserves the predicted amino acid sequence of the YopE 1-7 -Npt but abrogates secretion of the reporter protein. When introduced into the context of the full-length yopE gene, the single-nucleotide mutation reduces the type III injection of YopE into HeLa cells, even though the predicted amino acid sequence remains the same. Thus, yopE mRNA appears to encode a property that mediates the type III injection of YopE.

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confidence: 80%

A Synonymous Mutation in Yersinia enterocolitica yopE Affects the Function of the YopE Type III Secretion Signal

Ramamurthi

Schneewind

2005

J Bacteriol

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“…In fact, the length of the needles obtained from these mutants resembled the length of those observed in needle complexes obtained from the ΔinvJ mutant strain (16). It has been previously shown that secretion of InvJ through the TTSS is required for this regulatory protein to exert its function in needle complex assembly and substrate switching (26). To ascertain whether InvJ secretion was affected in the PrgJ mutants we examined the culture supernatants of these mutants for the presence of InvJ.…”

Section: Resultsmentioning

confidence: 78%

The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

Lefebre

Galán

2013

Proc. Natl. Acad. Sci. U.S.A.

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Type III secretion machines are essential for the biology of many bacteria that are pathogenic or symbiotic for animals, plants, or insects. They exert their function by delivering bacterial effector proteins into target eukaryotic cells. The core component of these machines is the needle complex, a multiprotein structure that spans the bacterial envelope and serves as a conduit for proteins that transit this secretion pathway. The needle complex is composed of a multiring base embedded in the bacterial envelope and a filament-like structure, the needle, that projects from the bacterial surface and is linked to the base by the inner rod. Assembly of the needle complex proceeds in a step-wise fashion that is initiated by the assembly of the base and is followed by the export of the building subunits for the needle and inner rod substructures. Once assembled, the needle complex reprograms its specificity and becomes competent for the secretion of effector proteins. Here through genetic, biochemical, and electron microscopy analyses of the Salmonella inner rod protein subunit PrgJ we present evidence that the assembly of the inner rod dictates the timing of substrate switching and needle length. Furthermore, the identification of mutations in PrgJ that specifically alter the hierarchy of protein secretion provides additional support for a complex role of the inner rod substructure in type III secretion.bacterial pathogenesis | organelle assembly | Salmonella pathogenesis

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“…The yscP-null mutant shows a leaky phenotype with regards to Yop secretion, since the mutant is still cytotoxic for HeLa cells. This is in contrast to fliK flagellar mutants and invJ mutants of Salmonella, which are impaired in substrate secretion (41,51). The reason behind this difference Mutations in the cytoplasmic region of YscU were introduced in trans into the yscP yscU-double-null strain.…”

Section: Discussionmentioning

confidence: 99%

YscP and YscU Regulate Substrate Specificity of theYersiniaType III Secretion System

et al. 2003

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Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein

Cited by 77 publications

References 33 publications

A Synonymous Mutation in Yersinia enterocolitica yopE Affects the Function of the YopE Type III Secretion Signal

A Synonymous Mutation in Yersinia enterocolitica yopE Affects the Function of the YopE Type III Secretion Signal

The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

YscP and YscU Regulate Substrate Specificity of theYersiniaType III Secretion System

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