Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.
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Structure of the TatC core of the twin-arginine protein transport systemThe Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine TranslocationGenetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.Abrogation of the twin arginine transport system in Salmonella enterica serovar Typhimurium leads to colonization defects during infection.Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET.Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Twin-Arginine Protein Translocation.The canonical twin-arginine translocase components are not required for secretion of folded green fluorescent protein from the ancestral strain of Bacillus subtilis.The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Initial assembly steps of a translocase for folded proteins.Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase.TatB functions as an oligomeric binding site for folded Tat precursor proteins.Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coliTransmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Mapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linkingMolecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding.Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.
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Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.
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article científic
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artigo científico
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bilimsel makale
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scientific article published on 22 September 2007
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vetenskaplig artikel
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Escherichia coli tatC mutation ...... e transporter signal peptides.
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Escherichia coli tatC mutation ...... e transporter signal peptides.
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Escherichia coli tatC mutation ...... e transporter signal peptides.
@en
Escherichia coli tatC mutation ...... e transporter signal peptides.
@nl
prefLabel
Escherichia coli tatC mutation ...... e transporter signal peptides.
@en
Escherichia coli tatC mutation ...... e transporter signal peptides.
@nl
P2860
P1476
Escherichia coli tatC mutation ...... e transporter signal peptides.
@en
P2093
Eva-Maria Strauch
George Georgiou
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P304
P356
10.1016/J.JMB.2007.09.050
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P577
2007-09-22T00:00:00Z