Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
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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 pathwayGenes required for completion of import of proteins into the endoplasmic reticulum in yeast.Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding proteinThe complete general secretory pathway in gram-negative bacteriaNucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli.Protein targeting to the bacterial cytoplasmic membrane.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.Mechanisms of protein localization.Cultured mammalian cells attach to the invasin protein of Yersinia pseudotuberculosis.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.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.A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.A mutation in a new gene, bglJ, activates the bgl operon in Escherichia coli K-12Catabolic repression of secB expression is positively controlled by cyclic AMP (cAMP) receptor protein-cAMP complexes at the transcriptional levelGreen fluorescent protein functions as a reporter for protein localization in Escherichia coli.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Folding LacZ in the periplasm of Escherichia coli.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.Trigger factor depletion or overproduction causes defective cell division but does not block protein export.Single-site chromosomal Tn5 insertions affect the export of pectolytic and cellulolytic enzymes in Erwinia chrysanthemi EC16.Escherichia coli SecB protein associates with exported protein precursors in vivoFunctional analysis of the signal recognition particle in Escherichia coli by characterization of a temperature-sensitive ffh mutant.Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.SecB is a bona fide generalized chaperone in Escherichia coliMultitasking SecB chaperones in bacteriaA yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum.SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Individual chaperones required for Yop secretion by YersiniaHeat-shock proteins can substitute for SecB function during protein export in Escherichia coli.One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.A little help from my friends: quality control of presecretory proteins in bacteria
P2860
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P2860
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
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1983 nî lūn-bûn
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name
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@ast
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@en
type
label
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@ast
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@en
prefLabel
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@ast
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@en
P2860
P1476
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.
@en
P2093
Beckwith J
Kumamoto CA
P2860
P304
P407
P577
1983-04-01T00:00:00Z