Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.
about
Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsStructure of the TatC core of the twin-arginine protein transport systemStructural model for the protein-translocating element of the twin-arginine transport systemStructural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric StructureTatBC-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.Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface.Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).Twin-Arginine Protein Translocation.Initial assembly steps of a translocase for folded proteins.In vivo experiments do not support the charge zipper model for Tat translocase assemblyTatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases.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-linkingThe Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes.Direct 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.The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.Protein Expression Modifications in Phage-Resistant Mutants of Aeromonas salmonicida after AS-A Phage Treatment.
P2860
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P2860
Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Early contacts between substra ...... n twin-arginine translocation.
@en
Early contacts between substra ...... n twin-arginine translocation.
@nl
type
label
Early contacts between substra ...... n twin-arginine translocation.
@en
Early contacts between substra ...... n twin-arginine translocation.
@nl
prefLabel
Early contacts between substra ...... n twin-arginine translocation.
@en
Early contacts between substra ...... n twin-arginine translocation.
@nl
P2093
P2860
P356
P1476
Early contacts between substra ...... n twin-arginine translocation.
@en
P2093
Julia Fröbel
Matthias Müller
Patrick Rose
P2860
P304
43679-43689
P356
10.1074/JBC.M111.292565
P407
P577
2011-10-31T00:00:00Z