The signal recognition particle receptor is a complex that contains two distinct polypeptide chains
about
The N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative chargesProtein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptorThe beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membraneThe similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevanceSignal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon.Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.Use of synthetic signal sequences to explore the protein export machinery.Protein targeting to the bacterial cytoplasmic membrane.The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.Targeting of rough endoplasmic reticulum membrane proteins and ribosomes in invertebrate neurons.Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum.Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway.Signal recognition particle (SRP), a ubiquitous initiator of protein translocation.Reconstitution of translocation-competent membrane vesicles from detergent-solubilized dog pancreas rough microsomesThe membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria.The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAsIntracellular traffic of newly synthesized proteins. Current understanding and future prospectsThe protein translocation systems in plants - composition and variability on the example of Solanum lycopersicumMolecular mechanism of co-translational protein targeting by the signal recognition particleYidC, a newly defined evolutionarily conserved protein, mediates membrane protein assembly in bacteria.Translocation of proteins across and integration of membrane proteins into the rough endoplasmic reticulum.Network Topologies Decoding Cervical Cancer.Full-length prepro-alpha-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated.Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor.SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum.A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.Antiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides.Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membraneGTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor.Dynamics of co-translational protein targeting.ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein.Ribosome binding to the endoplasmic reticulum: a 180-kD protein identified by crosslinking to membrane-bound ribosomes is not required for ribosome binding activityRibosome-binding protein p34 is a member of the leucine-rich-repeat-protein superfamilyProtein affinity chromatography with purified yeast DNA polymerase alpha detects proteins that bind to DNA polymerase.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.Protein export in prokaryotes and eukaryotes. Theme with variations.Post-translational import of protein into the endoplasmic reticulum of a trypanosome: an in vitro system for discovery of anti-trypanosomal chemical entities.Signal recognition particle: an essential protein-targeting machine.
P2860
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P2860
The signal recognition particle receptor is a complex that contains two distinct polypeptide chains
description
1986 nî lūn-bûn
@nan
1986 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
The signal recognition particl ...... wo distinct polypeptide chains
@ast
The signal recognition particl ...... wo distinct polypeptide chains
@en
The signal recognition particl ...... wo distinct polypeptide chains
@nl
type
label
The signal recognition particl ...... wo distinct polypeptide chains
@ast
The signal recognition particl ...... wo distinct polypeptide chains
@en
The signal recognition particl ...... wo distinct polypeptide chains
@nl
prefLabel
The signal recognition particl ...... wo distinct polypeptide chains
@ast
The signal recognition particl ...... wo distinct polypeptide chains
@en
The signal recognition particl ...... wo distinct polypeptide chains
@nl
P2093
P2860
P356
P1476
The signal recognition particl ...... wo distinct polypeptide chains
@en
P2093
P2860
P304
P356
10.1083/JCB.103.4.1167
P407
P577
1986-10-01T00:00:00Z