ATP is essential for protein translocation into Escherichia coli membrane vesicles.
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SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationPhospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channelsSecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificityThe complete general secretory pathway in gram-negative bacteriaNucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli.SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms.Binding of a soluble factor of Escherichia coli to preproteins does not require ATP and appears to be the first step in protein export.Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology.The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling.Sec-dependent membrane protein biogenesis: SecYEG, preprotein hydrophobicity and translocation kinetics control the stop-transfer function.Both ATP and an energized inner membrane are required to import a purified precursor protein into mitochondriaImport of an incompletely folded precursor protein into isolated mitochondria requires an energized inner membrane, but no added ATP.Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels.Structure and function of the bacterial Sec translocon.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent formBiochemical evidence for the secY24 defect in Escherichia coli protein translocation and its suppression by soluble cytoplasmic factors.Protein import into chloroplasts requires a chloroplast ATPaseRing-like pore structures of SecA: implication for bacterial protein-conducting channels.Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesiclesSecA: a potential antimicrobial target.Isolation and analysis of dominant secA mutations in Escherichia coliTobramycin uptake in Escherichia coli is driven by either electrical potential or ATPTemperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process.Requirement of heat-labile cytoplasmic protein factors for posttranslational translocation of OmpA protein precursors into Escherichia coli membrane vesicles.Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysisIn vitro insertion of leader peptidase into Escherichia coli membrane vesicles.Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potentialPrepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles.Roles of H+-ATPase and proton motive force in ATP-dependent protein translocation in vitro.Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coliEffects of nucleotides on ATP-dependent protein translocation into Escherichia coli membrane vesiclesDissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.
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P2860
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 1985
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@en
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@nl
type
label
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@en
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@nl
prefLabel
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@en
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@nl
P2860
P356
P1476
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
@en
P2860
P304
P356
10.1073/PNAS.82.13.4384
P407
P577
1985-07-01T00:00:00Z