Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationCytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecBThe Sec-dependent pathwayReversible formation of on-pathway macroscopic aggregates during the folding of maltose binding proteinBiophysical characterization of the influence of salt on tetrameric SecB.The complete general secretory pathway in gram-negative bacteriaSubstrate specificity of the SecB chaperone.SecYEG assembles into a tetramer to form the active protein translocation channel.Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.Protein targeting to the bacterial cytoplasmic membrane.Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.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.Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme.Sec-dependent membrane protein biogenesis: SecYEG, preprotein hydrophobicity and translocation kinetics control the stop-transfer function.PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation.The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB proteinCatabolic repression of secB expression is positively controlled by cyclic AMP (cAMP) receptor protein-cAMP complexes at the transcriptional levelStructure and function of the bacterial Sec translocon.Translocation can drive the unfolding of a preprotein domain.A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.Sec-dependent protein export and the involvement of the molecular chaperone SecB.Escherichia coli SecB protein associates with exported protein precursors in vivoDetergent 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.The structural view of bacterial translocation-specific chaperone SecB: implications for function.Evaluating the oligomeric state of SecYEG in preprotein translocase.SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein.Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules.Combined effects of the signal sequence and the major chaperone proteins on the export of human cytokines in Escherichia coliUsing superfolder green fluorescent protein for periplasmic protein localization studies.Extracellular production of a novel endo-β-agarase AgaA from Pseudomonas vesicularis MA103 that cleaves agarose into neoagarotetraose and neoagarohexaoseDemonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning.Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.Regulation by proteolysis: energy-dependent proteases and their targets.Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli.PrlA and PrlG suppressors reduce the requirement for signal sequence recognitionA mutation of Escherichia coli SecA protein that partially compensates for the absence of SecB.Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli
P2860
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P2860
Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.
description
1988 nî lūn-bûn
@nan
1988 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Purified secB protein of Esche ...... tose-binding protein in vitro.
@ast
Purified secB protein of Esche ...... tose-binding protein in vitro.
@en
type
label
Purified secB protein of Esche ...... tose-binding protein in vitro.
@ast
Purified secB protein of Esche ...... tose-binding protein in vitro.
@en
prefLabel
Purified secB protein of Esche ...... tose-binding protein in vitro.
@ast
Purified secB protein of Esche ...... tose-binding protein in vitro.
@en
P2093
P2860
P356
P1476
Purified secB protein of Esche ...... tose-binding protein in vitro.
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.23.8978
P407
P577
1988-12-01T00:00:00Z