Location and mobility of twin arginine translocase subunits in the Escherichia coli plasma membrane.
about
Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsSupramolecular assemblies underpin turnover of outer membrane proteins in bacteria.Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.Stoichiometry and turnover in single, functioning membrane protein complexes.TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex.Absence of long-range diffusion of OmpA in E. coli is not caused by its peptidoglycan binding domain.TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.Calcium Enhances Bile Salt-Dependent Virulence Activation in Vibrio cholerae.Subcellular localization of TatAd of Bacillus subtilis depends on the presence of TatCd or TatCy.Polar localization of the autotransporter family of large bacterial virulence proteins.Diffusion of green fluorescent protein in three cell environments in Escherichia coli.Green fluorescent chimeras indicate nonpolar localization of pullulanase secreton components PulL and PulM.Type II secretion system secretin PulD localizes in clusters in the Escherichia coli outer membrane.Independent mobility of proteins and lipids in the plasma membrane of Escherichia coli.Sec- and Tat-dependent translocation of beta-lactamases across the Escherichia coli inner membrane.In vivo associations of Escherichia coli NarJ with a peptide of the first 50 residues of nitrate reductase catalytic subunit NarG.Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid.Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network.Recombinant expression of tatABC and tatAC results in the formation of interacting cytoplasmic TatA tubes in Escherichia coli.
P2860
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P2860
Location and mobility of twin arginine translocase subunits in the Escherichia coli plasma membrane.
description
2005 nî lūn-bûn
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2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
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2005年學術文章
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name
Location and mobility of twin ...... herichia coli plasma membrane.
@de
Location and mobility of twin ...... herichia coli plasma membrane.
@en
Location and mobility of twin ...... herichia coli plasma membrane.
@nl
type
label
Location and mobility of twin ...... herichia coli plasma membrane.
@de
Location and mobility of twin ...... herichia coli plasma membrane.
@en
Location and mobility of twin ...... herichia coli plasma membrane.
@nl
prefLabel
Location and mobility of twin ...... herichia coli plasma membrane.
@de
Location and mobility of twin ...... herichia coli plasma membrane.
@en
Location and mobility of twin ...... herichia coli plasma membrane.
@nl
P2093
P2860
P356
P1476
Location and mobility of twin ...... herichia coli plasma membrane.
@en
P2093
Anja Nenninger
Colin Robinson
Conrad W Mullineaux
Nicola Ray
P2860
P304
17961-17968
P356
10.1074/JBC.M413521200
P407
P577
2005-02-23T00:00:00Z