Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationThe Sec-dependent pathwayPromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneThe complete general secretory pathway in gram-negative bacteriaInsights into the structure and assembly of Escherichia coli outer membrane protein ASelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoRotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Chaperone domains convert prolyl isomerases into generic catalysts of protein folding.SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.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.Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation.A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes.ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB proteinThe secD locus of E.coli codes for two membrane proteins required for protein export.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Translocation can drive the unfolding of a preprotein domain.Trigger factor depletion or overproduction causes defective cell division but does not block protein export.In vivo analysis of the overlapping functions of DnaK and trigger factorSpecific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.Immunoproteomic identification of immunogenic proteins in Cronobacter sakazakii strain BAA-894.Multitasking SecB chaperones in bacteriaTrigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease.Revisiting the interaction between the chaperone Skp and lipopolysaccharideCarbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.A little help from my friends: quality control of presecretory proteins in bacteriaThe folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export.Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process.Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.Requirement of heat-labile cytoplasmic protein factors for posttranslational translocation of OmpA protein precursors into Escherichia coli membrane vesicles.Synthesis of an Escherichia coli protein carrying a signal peptide mutation causes depolarization of the cytoplasmic membrane potential.In vitro insertion of leader peptidase into Escherichia coli membrane vesicles.Role of the leader peptide of maltose-binding protein in two steps of the export processElectrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coliInteraction of SecB with intermediates along the folding pathway of maltose-binding protein.Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.
P2860
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P2860
Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form
description
1987 nî lūn-bûn
@nan
1987 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@ast
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@en
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@nl
type
label
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@ast
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@en
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@nl
prefLabel
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@ast
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@en
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@nl
P2860
P356
P1476
Trigger factor: a soluble prot ...... mbrane-assembly-competent form
@en
P2093
P2860
P304
P356
10.1073/PNAS.84.15.5216
P407
P577
1987-08-01T00:00:00Z