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- W2886095627 abstract "Abstract In bacteria, the twin-arginine translocation (Tat) pathway allows the export of folded proteins through the inner membrane. Proteins targeted to this system are synthesized with N-terminal signal peptides bearing a conserved twin-arginine motif. The Tat pathway is critical for many bacterial processes including pathogenesis and virulence. However, the full set of Tat substrates is unknown in many bacteria, and the reliability of in silico prediction methods largely uncertain. In this work, we performed a combination of in silico analysis and experimental validation to identify a core set of Tat substrates in the opportunistic pathogen Pseudomonas aeruginosa . In silico analysis predicted 44 putative Tat signal peptides in the P. aeruginosa PA14 proteome. We developed an improved amidase-based Tat reporter assay to show that 33 of these are real Tat signal peptides. In addition, in silico analysis of the full translated genome revealed a Tat candidate with a missassigned start codon. We showed that it is a new periplasmic protein in P. aeruginosa . Altogether we discovered and validated 34 Tat substrates. These show little overlap with Escherichia coli Tat substrates, and functional analysis points to a general role for the P. aeruginosa Tat system in the colonization of environmental niches and pathogenicity." @default.
- W2886095627 created "2018-08-22" @default.
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- W2886095627 date "2018-08-09" @default.
- W2886095627 modified "2023-10-14" @default.
- W2886095627 title "Genome wide identification and experimental validation of Pseudomonas aeruginosa Tat substrates" @default.
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- W2886095627 doi "https://doi.org/10.1038/s41598-018-30393-x" @default.
- W2886095627 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6085387" @default.
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