Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.
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Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membraneThe structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting siteThe crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleftLipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein TargetingEvolution from the Prokaryotic to the Higher Plant Chloroplast Signal Recognition Particle: The Signal Recognition Particle RNA Is Conserved in Plastids of a Wide Range of Photosynthetic OrganismsHow bacteria maintain location and number of flagella?The social fabric of the RNA degradosomePredominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Archaea signal recognition particle shows the way.Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.Identification of cold-inducible inner membrane proteins of the psychrotrophic bacterium, Shewanella livingstonensis Ac10, by proteomic analysis.SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein.Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Molecular mechanism of co-translational protein targeting by the signal recognition particleProtein targeting by the signal recognition particle.Mechanisms of integral membrane protein insertion and foldingRibosome-SRP-FtsY cotranslational targeting complex in the closed stateMammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationSecYEG activates GTPases to drive the completion of cotranslational protein targeting.A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathwaySRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Breaking on through to the other side: protein export through the bacterial Sec system.Signal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Fidelity of cotranslational protein targeting by the signal recognition particle.Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysisATPase and GTPase Tangos Drive Intracellular Protein Transport.Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivoElectrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY.Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting.Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.Identification and in silico analysis of helical lipid binding regions in proteins belonging to the amphitropic protein family.Investigation into FlhFG reveals distinct features of FlhF in regulating flagellum polarity in Shewanella oneidensis.Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.
P2860
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P2860
Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
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2007年學術文章
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2007年學術文章
@zh-hant
name
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@en
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@nl
type
label
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@en
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@nl
prefLabel
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@en
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@nl
P2093
P2860
P50
P356
P1476
Escherichia coli signal recogn ...... ane-binding amphipathic helix.
@en
P2093
Irmgard Sinning
Liat Bahari
Richard Parlitz
P2860
P304
32176-32184
P356
10.1074/JBC.M705430200
P407
P577
2007-08-28T00:00:00Z