Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.
about
Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organismsProtein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum.The complete general secretory pathway in gram-negative bacteriaUse of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidaseExport of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.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.lac permease of Escherichia coli: topology and sequence elements promoting membrane insertionSite-specific antibodies against the PrlA (secY) protein of Escherichia coli inhibit protein export by interfering with plasma membrane binding of preproteins.The secD locus of E.coli codes for two membrane proteins required for protein export.Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysisA signal sequence is not required for protein export in prlA mutants of Escherichia coliModeling the effects of prl mutations on the Escherichia coli SecY complex.PrlA suppressor mutations cluster in regions corresponding to three distinct topological domainsGO-PROMTO illuminates protein membrane topologies of glycan biosynthetic enzymes in the Golgi apparatus of living tissues.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.Positively charged amino acid residues can act as topogenic determinants in membrane proteinsFtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit.Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase.Demonstration of a specific Escherichia coli SecY-signal peptide interactionDifferent modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex.Export of FepA::PhoA fusion proteins to the outer membrane of Escherichia coli K-12One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.PrlA and PrlG suppressors reduce the requirement for signal sequence recognitionprlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli.In vivo studies of the role of SecA during protein export in Escherichia coliAlkaline phosphatase fusions: sensors of subcellular locationA protein required for transcriptional regulation of Agrobacterium virulence genes spans the cytoplasmic membrane.Temperature-sensitive sec mutants of Escherichia coli: inhibition of protein export at the permissive temperature.Genetic studies on the inability of beta-galactosidase to be translocated across the Escherichia coli cytoplasmic membrane.Characterization of cold-sensitive secY mutants of Escherichia coliA novel membrane-associated threonine permease encoded by the tdcC gene of Escherichia coli.Role of the cytoplasmic segments of Sec61alpha in the ribosome-binding and translocation-promoting activities of the Sec61 complexActivation of a bacterial lipase by its chaperoneComponent specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways.Genetic and biochemical evaluation of eucaryotic membrane protein topology: multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductaseIsolation and analysis of novel mutants of Escherichia coli prlA (secY).
P2860
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P2860
Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.
description
1987 nî lūn-bûn
@nan
1987 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի նոյեմբերին 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
Topology analysis of the SecY ...... in export in Escherichia coli.
@ast
Topology analysis of the SecY ...... in export in Escherichia coli.
@en
type
label
Topology analysis of the SecY ...... in export in Escherichia coli.
@ast
Topology analysis of the SecY ...... in export in Escherichia coli.
@en
prefLabel
Topology analysis of the SecY ...... in export in Escherichia coli.
@ast
Topology analysis of the SecY ...... in export in Escherichia coli.
@en
P2860
P1433
P1476
Topology analysis of the SecY ...... ein export in Escherichia coli
@en
P2860
P304
P356
10.1002/J.1460-2075.1987.TB02670.X
P407
P577
1987-11-01T00:00:00Z