The twin‐arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in <i>Legionella pneumophila</i>

Buck, Emmy De; Vranckx, Leen; Meyen, Eef; Maes, Liesbeth; Vandersmissen, L; Anné, Jozef; Lammertyn, Elke

doi:10.1016/j.febslet.2006.12.022

Cited by 36 publications

(31 citation statements)

References 30 publications

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“…This is fully consistent with our observations that mutation of the AtRip Tat targeting signal and also that AtRip requires a ΔpH for assembly. Rip proteins of chloroplasts and bacteria have also been demonstrated previously to require a Tat pathway for proper insertion (Molik et al, 2001;Aldridge et al, 2008;Bachmann et al, 2006;De Buck et al, 2007). These observations are strengthened by the correlation of mitochondrial Tat proteins with the absence of a complete Bcs1 protein in a variety of organisms.…”

Section: Discussionsupporting

confidence: 62%

Plant mitochondria contain the protein translocase subunits TatB and TatC

Carrie

Weißenberger

Soll

2016

Journal of Cell Science

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Twin-arginine translocation (Tat) pathways have been wellcharacterized in bacteria and chloroplasts. Genes encoding a TatC protein are found in almost all plant mitochondrial genomes but to date these have not been extensively investigated. For the first time it could be demonstrated that this mitochondrial-encoded TatC is a functional gene that is translated into a protein in the model plant Arabidopsis thaliana. A TatB-like subunit localized to the inner membrane was also identified that is nuclear-encoded and is essential for plant growth and development, indicating that plants potentially require a Tat pathway for mitochondrial biogenesis.

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Section: Discussionsupporting

confidence: 62%

Plant mitochondria contain the protein translocase subunits TatB and TatC

Carrie

Weißenberger

Soll

2016

Journal of Cell Science

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“…The alignments of MdfA from Y. pseudotuberculosis and E. coli revealed that they had a very high level of similarity (73.3% identity), but the E. coli MdfA does not have an RR motif in the N terminus and the Yersinia MdfA has 6 additional amino acid residues in the N-terminal sequence with an RR motif. Since the protein is not predicted to have any periplasmic domains, we find it unlikely that MdfA is a Tat substrate (44,48). fliY is the first gene in a putative operon (fliY yecS yecC) encoding proteins with a suggested function in cysteine transport that were previously identified in E. coli (49).…”

Section: Discussionmentioning

confidence: 99%

The Tat Substrate SufI Is Critical for the Ability of Yersinia pseudotuberculosis To Cause Systemic Infection

et al. 2017

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The twin arginine translocation (Tat) system targets folded proteins across the inner membrane and is crucial for virulence in many important humanpathogenic bacteria. Tat has been shown to be required for the virulence of Yersinia pseudotuberculosis, and we recently showed that the system is critical for different virulence-related stress responses as well as for iron uptake. In this study, we wanted to address the role of the Tat substrates in in vivo virulence. Therefore, 22 genes encoding potential Tat substrates were mutated, and each mutant was evaluated in a competitive oral infection of mice. Interestingly, a ΔsufI mutant was essentially as attenuated for virulence as the Tat-deficient strain. We also verified that SufI was Tat dependent for membrane/periplasmic localization in Y. pseudotuberculosis. In vivo bioluminescent imaging of orally infected mice revealed that both the ΔsufI and ΔtatC mutants were able to colonize the cecum and Peyer's patches (PPs) and could spread to the mesenteric lymph nodes (MLNs). Importantly, at this point, neither the ΔtatC mutant nor the ΔsufI mutant was able to spread systemically, and they were gradually cleared. Immunostaining of MLNs revealed that both the ΔtatC and ΔsufI mutants were unable to spread from the initial infection foci and appeared to be contained by neutrophils, while wild-type bacteria readily spread to establish multiple foci from day 3 postinfection. Our results show that SufI alone is required for the establishment of systemic infection and is the major cause of the attenuation of the ΔtatC mutant.KEYWORDS Yersinia pseudotuberculosis, Tat pathway, virulence, SufI, mesenteric lymph nodes, neutrophils T he genus Yersinia includes three species that are pathogenic to humans: Yersinia pestis, the causative agent of plague, and the two enteropathogens Y. enterocolitica and Y. pseudotuberculosis, which normally cause a self-limiting disease with symptoms ranging from mild diarrhea, enterocolitis, septicemia, and mesenteric lymphadenitis to reactive arthritis in humans after ingestion of contaminated food or water (1). Once it is ingested, Y. pseudotuberculosis traverses the epithelial barrier through M cells and infects the associated lymphoid tissues, such as Peyer's patches (PPs) and cecal patches, and later spreads to the mesenteric lymph nodes (MLNs). Although the infection is usually self-limited in humans, the infection caused by the two enteropathogenic Yersinia species in mice readily progresses to become systemic and disseminates to the spleen and liver (2). The main virulence arsenal of Yersinia is the type III secretion system (T3SS), which is encoded by an ϳ70-kb virulence plasmid. The T3SS enables the translocation of virulence effector proteins directly into the cytosol of the target host cell, which results in the disruption of host signaling and early immune

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“…41 One of the two signal peptides that scored positive for agarase export is derived from QcrA, which is the B. subtilis homologue of the Rieske iron sulfur protein, a known Tat substrate in plants 23 and recently also shown to be a Tat substrate in the bacteria Legionella pneumophila and Paracoccus denitrificans. 32,43 Interestingly, the Rieske proteins have uncleaved signal anchors and this seems to be true also for B. subtilis QcrA since the consensus signal peptidase cleavage motifs are absent from this protein. 44 Our findings therefore suggest that normally uncleaved twin-arginine signal peptides may also be positively identified as Tat-targeting sequences with the agarase reporter system.…”

Section: A Naturally Occurring Variant Tat Signal Peptide Can Mediatementioning

confidence: 90%

A Facile Reporter System for the Experimental Identification of Twin-Arginine Translocation (Tat) Signal Peptides from All Kingdoms of Life

Widdick

Eijlander

Dijl

et al. 2008

Journal of Molecular Biology

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The twin‐arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila

Cited by 36 publications

References 30 publications

Plant mitochondria contain the protein translocase subunits TatB and TatC

Plant mitochondria contain the protein translocase subunits TatB and TatC

The Tat Substrate SufI Is Critical for the Ability of Yersinia pseudotuberculosis To Cause Systemic Infection

A Facile Reporter System for the Experimental Identification of Twin-Arginine Translocation (Tat) Signal Peptides from All Kingdoms of Life

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