TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency

PloS One
Johannes TaubertThomas Brüser

Abstract

The Tat system can transport folded, signal peptide-containing proteins (Tat substrates) across energized membranes of prokaryotes and plant plastids. A twin-arginine motif in the signal peptide of Tat substrates is recognized by TatC-containing complexes, and TatA permits the membrane passage. Often, as in the model Tat systems of Escherichia coli and plant plastids, a third component - TatB - is involved that resembles TatA but has a higher affinity to TatC. It is not known why most TatA dissociates from TatBC complexes in vivo and distributes more evenly in the membrane. Here we show a TatBC-independent substrate-binding to TatA from Escherichia coli, and we provide evidence that this binding enhances Tat transport. First hints came from in vivo cross-linking data, which could be confirmed by affinity co-purification of TatA with the natural Tat substrates HiPIP and NrfC. Two positions on the surface of HiPIP could be identified that are important for the TatA interaction and transport efficiency, indicating physiological relevance of the interaction. Distributed TatA thus may serve to accompany membrane-interacting Tat substrates to the few TatBC spots in the cells.

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Citations

Jan 24, 2018·Scientific Reports·Ekaterina EimerMatthias Müller
Oct 21, 2015·The Journal of Biological Chemistry·Ekaterina EimerMatthias Müller
Apr 14, 2018·Engineering in Life Sciences·Gabriele R M Kleiner-GroteKarl Friehs
Feb 23, 2017·Proceedings of the National Academy of Sciences of the United States of America·Qi HuangTracy Palmer
Jun 20, 2019·EcoSal Plus·Kelly M FrainColin Robinson
Aug 31, 2021·Frontiers in Microbiology·Denise Mehner-BreitfeldThomas Brüser

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Methods Mentioned

BETA
Cross-linking analysis
Size exclusion chromatography
electron microscopy
peptide exchange
surface
biosensors
X-ray
PCR

Software Mentioned

MARTINI
pEvol System
GROMACS

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