Subunit composition and in vivo substrate-binding characteristics of Escherichia coli Tat protein complexes expressed at native levels.
about
The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like StructureVariable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.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 nicheStoichiometry for binding and transport by the twin arginine translocation systemTwo electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery.Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI.Twin-arginine-dependent translocation of folded proteins.Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).Twin-Arginine Protein Translocation.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.The Tat Substrate SufI Is Critical for the Ability of Yersinia pseudotuberculosis To Cause Systemic Infection.The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.TatB functions as an oligomeric binding site for folded Tat precursor proteins.Substrate-triggered position switching of TatA and TatB during Tat transport in Escherichia coli.Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coliTatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli.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-linkingCysteine scanning mutagenesis and topological mapping of the Escherichia coli twin-arginine translocase TatC Component.Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes.A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.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.Cysteine scanning mutagenesis and disulfide mapping studies of the TatA component of the bacterial twin arginine translocase.
P2860
Q27653378-58B60358-10F3-420A-A7FF-50ABA87AF328Q30483980-B12FDBBC-99EB-423A-A8E4-27F9C1FA85E6Q33532602-42A12381-4EAF-474F-8245-2D55F4727026Q34326584-654A52C3-6D5D-49D2-B1E7-731C318B3E9BQ35043567-0EB0AB00-4938-490C-85FA-104B8007A559Q35962289-FF87ACE2-CAE5-4BA0-BC65-8C74A9481251Q36119522-E5602585-0BD5-4558-B00D-7D95EFA92C35Q37146697-3E2819B3-9EC8-47CF-80BD-B6A647E9D073Q37404850-F50B18AA-A234-4E43-8A5D-56C2D130F906Q37993035-DFD03DD2-539E-4370-898B-A18F3D6B1B6FQ38480343-FC3EB15C-6A43-4F76-A403-00500B3D211AQ38819418-B92B68F0-CCE3-42AD-A36B-6E9599E8701AQ39936045-B0CDC11A-2698-42A0-8F17-6B9EB551C0F3Q40361015-3642B9BD-F6CA-4209-8A21-DDD2097114DEQ40796436-8E264034-A74B-4DC9-8FA4-B753B8F31731Q41440989-0DC3A14D-BECA-47C7-AD88-F4BFE144AFD4Q41567229-571EAA73-FC8C-4804-80B9-E6CF1508761CQ41871793-7EB7ED32-5A4C-42BA-9727-F26C5623A553Q41895626-89BE20AA-D97B-478E-B991-26E6ACCA8AF7Q41913286-9F58D43E-171F-4015-8731-07C7AD51E314Q42140993-F4DEBAEA-9D29-4329-BD6C-B9BA0A9141ACQ42412505-7B6E26E8-AD67-40C9-B02B-DF64D647F8AFQ42859956-3B540641-73BD-4BDA-90DB-243472235DC3Q47270644-E6BACBEB-0D28-459D-88FE-9801DA193349Q50995875-02819650-CDFC-4F9A-9FB3-E4B94168C00BQ52338994-01150914-9599-4C46-99A9-11A275BC3700Q54439818-8425B0C5-8756-4024-ABE9-FA3BC71D72D5
P2860
Subunit composition and in vivo substrate-binding characteristics of Escherichia coli Tat protein complexes expressed at native levels.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Subunit composition and in viv ...... es expressed at native levels.
@en
Subunit composition and in viv ...... es expressed at native levels.
@nl
type
label
Subunit composition and in viv ...... es expressed at native levels.
@en
Subunit composition and in viv ...... es expressed at native levels.
@nl
prefLabel
Subunit composition and in viv ...... es expressed at native levels.
@en
Subunit composition and in viv ...... es expressed at native levels.
@nl
P50
P1433
P1476
Subunit composition and in viv ...... es expressed at native levels.
@en
P2093
Grant Buchanan
P2860
P304
P356
10.1111/J.1742-4658.2006.05554.X
P407
P577
2006-12-01T00:00:00Z