Details
| Original language | English |
|---|---|
| Article number | 0119761 |
| Journal | PLOS ONE |
| Volume | 10 |
| Issue number | 3 |
| Publication status | Published - 16 Mar 2015 |
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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In: PLOS ONE, Vol. 10, No. 3, 0119761, 16.03.2015.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - TatBC-Independent TatA/Tat substrate interactions contribute to transport efficiency
AU - Taubert, Johannes
AU - Hou, Bo
AU - Risselada, H. Jelger
AU - Mehner, Denise
AU - Lünsdorf, Heinrich
AU - Grubmüller, Helmut
AU - Brüser, Thomas
N1 - Funding information: We thank Jana Behrendt for strain JBdBC, Sybille Traupe for excellent technical assistance, Peter G. Schultz for donation of the pEvol system, Andreas Kuhn for YidC antibodies, and Hauke Lilie for helpful discussion. This work was funded by the Deutsche Forschungsgemeinschaft (GRK 1026: „Conformational transitions during macromolecular interactions“).
PY - 2015/3/16
Y1 - 2015/3/16
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84924942565&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0119761
DO - 10.1371/journal.pone.0119761
M3 - Article
C2 - 25774531
AN - SCOPUS:84924942565
VL - 10
JO - PLOS ONE
JF - PLOS ONE
SN - 1932-6203
IS - 3
M1 - 0119761
ER -