The Tat system of Gram-positive bacteria

Goosens, Vivianne J.; Monteferrante, Carmine G.; Dijl, Jan Maarten van

doi:10.1016/j.bbamcr.2013.10.008

Cited by 69 publications

(64 citation statements)

References 153 publications

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“…In cells overexpressing TatE-GFP, the major TatE-immunoreactive material had the expected molecular mass of the TatE-GFP fusion (approximately 37 kDa; Fig. 2A, lanes [3][4][5][6]. Expression of TatE-GFP did not noticeably influence the amount of the 9-kDa TatE band, demonstrating stability of the TatE-GFP construct.…”

Section: Substrate-dependent Relocation Of Tate From a Uniform Distrimentioning

confidence: 93%

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TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases

Eimer¹,

Fröbel²,

Blümmel

et al. 2015

Journal of Biological Chemistry

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Background: Twin-arginine translocases, which transport folded proteins across cellular membranes, often consist of three proteins, TatA, TatB, and TatC, but sometimes have an additional TatE available. Results: TatE associates with active translocases and forms direct contacts with TatA, TatB, and TatC. Conclusion: TatE is a regular constituent of twin-arginine translocases. Significance: We elucidate a functional interplay of the paralogous proteins TatA and TatE.

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Section: Substrate-dependent Relocation Of Tate From a Uniform Distrimentioning

confidence: 93%

“…[1][2][3][4][5][6]. Whereas TatC is a hexahelical membrane protein (7,8), TatA, TatB, and TatE consist of only one transmembrane helix, followed by an amphipathic helix and an unstructured C terminus on the cis side of the membrane.…”

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confidence: 99%

TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases

Eimer¹,

Fröbel²,

Blümmel

et al. 2015

Journal of Biological Chemistry

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“…The minimal translocation complex found in Gram-positive bacteria and archaea consists of two proteins of the TatA and TatC family of integral membrane proteins. For some Gram-negative bacteria, including Escherichia coli, another TatA family protein denoted TatB is also required (6,7). The translocation process of the Tat pathway is energized by the electrochemical potential (Δp) of the membrane (8).…”

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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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“…First, the twin-arginine protein translocation (Tat) pathway signal protein was downregulated 2.7 fold in response to quercetin (Table 1), yet upregulated 2.3 fold in response to naringenin (Table 4). The Tat system is responsible for the movement of large, folded proteins into or through the cell wall [47,48]. Second, the ABC transporter ATP-binding protein was upregulated 2 fold for LGG treated with quercetin (Table 2) and downregulated 2.2 fold for LGG treated with naringenin (Table 3).…”

Section: Discussionmentioning

confidence: 99%

Genetic Expression Profile Analysis of the Temporal Inhibition of Quercetin and Naringenin on Lactobacillus Rhamnosus GG

Liu¹,

Firrman²

2016

J Prob Health

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Plant polyphenols quercetin and naringenin are considered healthy dietary compounds; however, little is known of their effect on the probiotic Lactobacillus rhamnosus GG (LGG). In this study it was discovered that both quercetin and naringenin produced temporary inhibition of LGG growth, particularly at 8 hours post inoculation, with LGG eventually recovering from this suppression. The observed growth inhibition was regarded as a phenotypic response of LGG to the polyphenols; we hypothesized that the subsequent recovery was due to unknown, underlying genetic factors. The molecular response of LGG to quercetin and naringenin was determined through RNA analysis using the Helicos single molecule sequencing platform. The expression profiles of LGG grown in the presence of either quercetin or naringenin were divergent from each other, with only a few similarities, indicating that these polyphenols inhibit growth through separate mechanisms.LGG treated with quercetin demonstrated upregulation of genes associated with DNA repair and transcriptional regulation, and a decrease in expression of genes involved in metabolism and protein movement through the cell wall.LGG treated with naringenin resulted in an increase of genes associated with metabolism, and a decrease in genes involved in stress response. Results from this study demonstrate that there is a clear interaction between the polyphenols quercetin and naringenin and the probiotic LGG. The RNA expression analysis provides unique insight into the molecular response of LGG to quercetin and naringenin, revealing an identifiable pattern of gene expression.

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The Tat system of Gram-positive bacteria

Cited by 69 publications

References 153 publications

TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases

TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases

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

Genetic Expression Profile Analysis of the Temporal Inhibition of Quercetin and Naringenin on Lactobacillus Rhamnosus GG

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