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• W2050207946 startingPage "e9225" @default.
• W2050207946 abstract "The twin-arginine translocation (Tat) pathway is well known for its ability to export fully folded substrate proteins out of the cytoplasm of Gram-negative and Gram-positive bacteria. Studies of this mechanism in Escherichia coli have identified numerous transient protein-protein interactions that guide export-competent proteins through the Tat pathway. To visualize these interactions, we have adapted bimolecular fluorescence complementation (BiFC) to detect protein-protein interactions along the Tat pathway of living cells. Fragments of the yellow fluorescent protein (YFP) were fused to soluble and transmembrane factors that participate in the translocation process including Tat substrates, Tat-specific proofreading chaperones and the integral membrane proteins TatABC that form the translocase. Fluorescence analysis of these YFP chimeras revealed a wide range of interactions such as the one between the Tat substrate dimethyl sulfoxide reductase (DmsA) and its dedicated proofreading chaperone DmsD. In addition, BiFC analysis illuminated homo- and hetero-oligomeric complexes of the TatA, TatB and TatC integral membrane proteins that were consistent with the current model of translocase assembly. In the case of TatBC assemblies, we provide the first evidence that these complexes are co-localized at the cell poles. Finally, we used this BiFC approach to capture interactions between the putative Tat receptor complex formed by TatBC and the DmsA substrate or its dedicated chaperone DmsD. Our results demonstrate that BiFC is a powerful approach for studying cytoplasmic and inner membrane interactions underlying bacterial secretory pathways." @default.
• W2050207946 created "2016-06-24" @default.
• W2050207946 creator A5001198279 @default.
• W2050207946 creator A5052150279 @default.
• W2050207946 creator A5076324446 @default.
• W2050207946 creator A5081822200 @default.
• W2050207946 date "2010-02-16" @default.
• W2050207946 modified "2023-09-27" @default.
• W2050207946 title "Visualizing Interactions along the Escherichia coli Twin-Arginine Translocation Pathway Using Protein Fragment Complementation" @default.
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• W2050207946 doi "https://doi.org/10.1371/journal.pone.0009225" @default.
• W2050207946 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2821923" @default.
• W2050207946 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20169075" @default.
• W2050207946 hasPublicationYear "2010" @default.
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