Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY.
about
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 siteLipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein TargetingPredominant 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.Membrane protein biogenesis in Ffh- or FtsY-depleted Escherichia coli.Archaea signal recognition particle shows the way.Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.Protein targeting by the signal recognition particle.SRP 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.Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivoRational design of a fusion partner for membrane protein expression in E. coli.Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting.Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteinsSignal 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.Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The bacterial SRP receptor, FtsY, is activated on binding to the translocon.
P2860
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P2860
Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年學術文章
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name
Membrane targeting of ribosome ...... d separable functions of FtsY.
@en
Membrane targeting of ribosome ...... d separable functions of FtsY.
@nl
type
label
Membrane targeting of ribosome ...... d separable functions of FtsY.
@en
Membrane targeting of ribosome ...... d separable functions of FtsY.
@nl
prefLabel
Membrane targeting of ribosome ...... d separable functions of FtsY.
@en
Membrane targeting of ribosome ...... d separable functions of FtsY.
@nl
P2093
P2860
P356
P1476
Membrane targeting of ribosome ...... d separable functions of FtsY.
@en
P2093
Elena S Bochkareva
Irmgard Sinning
Liat Bahari
Richard Parlitz
P2860
P304
32168-32175
P356
10.1074/JBC.M705429200
P407
P577
2007-08-28T00:00:00Z