The enzymology of protein translocation across the Escherichia coli plasma membrane.
about
A polypeptide-DNA hybrid with selective linking capability applied to single molecule nano-mechanical measurements using optical tweezersStructure of the E. coli protein-conducting channel bound to a translating ribosomeMolecular characterization of an operon required for pertussis toxin secretionTransport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membraneSecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationABC transporters: bacterial exportersDeterminants of extracellular protein secretion in gram-negative bacteriaPAS7 encodes a novel yeast member of the WD-40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into peroxisomesPresequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix.Co-translational protein targeting by the signal recognition particleExpression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37RvIsolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathwayThe complete general secretory pathway in gram-negative bacteriaAlpha-crystallin can function as a molecular chaperoneOrigin of the 2-amino-2-deoxy-gluconate unit in Rhizobium leguminosarum lipid A. Expression cloning of the outer membrane oxidase LpxQLoss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant.Identification of protein secretion systems and novel secreted proteins in Rhizobium leguminosarum bv. viciae.Inter-species complementation of the translocon beta subunit requires only its transmembrane domain.PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation.Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.Deletion of the leader peptide of the mitochondrially encoded precursor of Saccharomyces cerevisiae cytochrome c oxidase subunit II.Transcriptional activation of ydeA, which encodes a member of the major facilitator superfamily, interferes with arabinose accumulation and induction of the Escherichia coli arabinose PBAD promoter.Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence.The bacterium's way for safe enlargement and division.Translocation can drive the unfolding of a preprotein domain.Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain lengthPrlA suppressor mutations cluster in regions corresponding to three distinct topological domainsA novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.Protein transport via amino-terminal targeting sequences: common themes in diverse systems.Ribosome-mediated translational pause and protein domain organizationEvidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyadFolding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies.Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.Use of alkaline phosphatase as a reporter polypeptide to study the role of the subtilin leader segment and the SpaT transporter in the posttranslational modifications and secretion of subtilin in Bacillus subtilis 168.Subunit dynamics in Escherichia coli preprotein translocase.Beta-galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli.SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membraneBiotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertionDelineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes
P2860
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P2860
The enzymology of protein translocation across the Escherichia coli plasma membrane.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@en
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@nl
type
label
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@en
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@nl
prefLabel
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@en
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@nl
P1476
The enzymology of protein translocation across the Escherichia coli plasma membrane.
@en
P2093
A J Driessen
P304
P356
10.1146/ANNUREV.BI.60.070191.000533
P577
1991-01-01T00:00:00Z