The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.

The Journal of Biological Chemistry
Agnes UlfigR Freudl

Abstract

The twin-arginine translocation (Tat) pathway transports folded proteins across bacterial membranes. Tat precursor proteins possess a conserved twin-arginine (RR) motif in their signal peptides that is involved in their binding to the Tat translocase, but some facets of this interaction remain unclear. Here, we investigated the role of the hydrophobic (h-) region of the Escherichia coli trimethylamine N-oxide reductase (TorA) signal peptide in TatBC receptor binding in vivo and in vitro We show that besides the RR motif, a minimal, functional h-region in the signal peptide is required for Tat-dependent export in Escherichia coli Furthermore, we identified mutations in the h-region that synergistically suppressed the export defect of a TorA[KQ]-30aa-MalE Tat reporter protein in which the RR motif was replaced with a lysine-glutamine pair. Strikingly, all suppressor mutations increased the hydrophobicity of the h-region. By systematically replacing a neutral residue in the h-region with various amino acids, we detected a positive correlation between the hydrophobicity of the h-region and the translocation efficiency of the resulting reporter variants. In vitro cross-linking of residues located in the periplasmically-oriented part...Continue Reading

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Nov 2, 2017·The Journal of Biological Chemistry·Anne-Sophie BlümmelJulia Fröbel
Jan 24, 2018·Scientific Reports·Ekaterina EimerMatthias Müller
Jan 24, 2020·Molecular Microbiology·Tracy Palmer, Phillip J Stansfeld
Aug 14, 2018·Photosynthesis Research·Christopher Paul NewCarole Dabney-Smith

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