TatB functions as an oligomeric binding site for folded Tat precursor proteins.
about
Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsIt takes two to tango: two TatA paralogues and two redox enzyme-specific chaperones are involved in the localization of twin-arginine translocase substrates in Campylobacter jejuni.Engineering antibody fitness and function using membrane-anchored display of correctly folded proteins.Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental nicheTatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET.Stoichiometry for binding and transport by the twin arginine translocation systemThe chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport.Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).The canonical twin-arginine translocase components are not required for secretion of folded green fluorescent protein from the ancestral strain of Bacillus subtilis.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.Initial assembly steps of a translocase for folded proteins.Transmembrane 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-linkingDirect interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts.A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Precursor-receptor interactions in the twin arginine protein transport pathway probed with a new receptor complex preparation.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.The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding.
P2860
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P2860
TatB functions as an oligomeric binding site for folded Tat precursor proteins.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
TatB functions as an oligomeric binding site for folded Tat precursor proteins.
@en
type
label
TatB functions as an oligomeric binding site for folded Tat precursor proteins.
@en
prefLabel
TatB functions as an oligomeric binding site for folded Tat precursor proteins.
@en
P2093
P2860
P356
P1476
TatB functions as an oligomeric binding site for folded Tat precursor proteins
@en
P2093
Anna-Carina Jungkamp
Matthias Müller
Michael Moser
Sascha Panahandeh
P2860
P304
P356
10.1091/MBC.E10-07-0585
P50
P577
2010-10-06T00:00:00Z