2.50
Hdl Handle:
http://hdl.handle.net/10033/550999
Title:
TatBC-Independent TatA/Tat Substrate Interactions Contribute to Transport Efficiency.
Authors:
Taubert, Johannes; Hou, Bo; Risselada, H Jelger; Mehner, Denise; Lünsdorf, Heinrich; Grubmüller, Helmut; Brüser, Thomas
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.
Citation:
TatBC-Independent TatA/Tat Substrate Interactions Contribute to Transport Efficiency. 2015, 10 (3):e0119761 PLoS ONE
Journal:
PloS one
Issue Date:
2015
URI:
http://hdl.handle.net/10033/550999
DOI:
10.1371/journal.pone.0119761
PubMed ID:
25774531
Type:
Article
Language:
en
ISSN:
1932-6203
Appears in Collections:
publications of the central unit for microscopy (ZEIM)

Full metadata record

DC FieldValue Language
dc.contributor.authorTaubert, Johannesen
dc.contributor.authorHou, Boen
dc.contributor.authorRisselada, H Jelgeren
dc.contributor.authorMehner, Deniseen
dc.contributor.authorLünsdorf, Heinrichen
dc.contributor.authorGrubmüller, Helmuten
dc.contributor.authorBrüser, Thomasen
dc.date.accessioned2015-04-30T09:08:40Zen
dc.date.available2015-04-30T09:08:40Zen
dc.date.issued2015en
dc.identifier.citationTatBC-Independent TatA/Tat Substrate Interactions Contribute to Transport Efficiency. 2015, 10 (3):e0119761 PLoS ONEen
dc.identifier.issn1932-6203en
dc.identifier.pmid25774531en
dc.identifier.doi10.1371/journal.pone.0119761en
dc.identifier.urihttp://hdl.handle.net/10033/550999en
dc.description.abstractThe 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.en
dc.language.isoenen
dc.titleTatBC-Independent TatA/Tat Substrate Interactions Contribute to Transport Efficiency.en
dc.typeArticleen
dc.identifier.journalPloS oneen
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