The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex.
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Targeting of lumenal proteins across the thylakoid membraneA minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexesVariable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.Formation of functional Tat translocases from heterologous componentsVisualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.Subunit organization in the TatA complex of the twin arginine protein translocase: a site-directed EPR spin labeling studyThe TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter.Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles.Two electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery.The bacterial twin-arginine translocation pathway.Twin arginine translocation in Yersinia.Use of folding modulators to improve heterologous protein production in Escherichia coli.Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Signal peptidase I: cleaving the way to mature proteins.The ins and outs of Mycobacterium tuberculosis protein export.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores.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.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway.Blue Native PAGE Analysis of Bacterial Secretion Complexes.The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Subcellular localization of TatAd of Bacillus subtilis depends on the presence of TatCd or TatCy.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 coliStructure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter.TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli.Large-scale translocation reversal within the thylakoid Tat system in vivo.The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules.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.Cysteine 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.Relaxed specificity of the Bacillus subtilis TatAdCd translocase in Tat-dependent protein secretion.Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts.Expression of the bifunctional Bacillus subtilis TatAd protein in Escherichia coli reveals distinct TatA/B-family and TatB-specific domains.
P2860
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P2860
The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex.
description
2004 nî lūn-bûn
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2004年の論文
@ja
2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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name
The Escherichia coli twin-argi ...... lexes and minor TatAB complex.
@en
The Escherichia coli twin-argi ...... lexes and minor TatAB complex.
@nl
type
label
The Escherichia coli twin-argi ...... lexes and minor TatAB complex.
@en
The Escherichia coli twin-argi ...... lexes and minor TatAB complex.
@nl
prefLabel
The Escherichia coli twin-argi ...... lexes and minor TatAB complex.
@en
The Escherichia coli twin-argi ...... lexes and minor TatAB complex.
@nl
P2093
P1476
The Escherichia coli twin-argi ...... plexes and minor TatAB complex
@en
P2093
Claire M L Barrett
Colin Robinson
Joanne Oates
Katheryne G Byrne
P304
P356
10.1016/J.JMB.2004.11.047
P407
P577
2004-12-13T00:00:00Z