Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation
about
A tale of two GTPases in cotranslational protein targetingStructures of the E. coli translating ribosome with SRP and its receptor and with the translocon.The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting siteNucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase FfhStructural insights into tail-anchored protein binding and membrane insertion by Get3The Crystal Structure of the Signal Recognition Particle in Complex with Its ReceptorLipids 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 OrganismsStructural basis of signal sequence surveillance and selection by the SRP–FtsY complexThe Structural Basis of FtsY Recruitment and GTPase Activation by SRP RNAYlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutansPredominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.Activated GTPase movement on an RNA scaffold drives co-translational protein targetingInefficient translocation of preproinsulin contributes to pancreatic β cell failure and late-onset diabetes.Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.Molecular mechanism of co-translational protein targeting by the signal recognition particleProtein targeting by the signal recognition particle.Regulation by a chaperone improves substrate selectivity during cotranslational protein targetingTranslation elongation regulates substrate selection by the signal recognition particle.Fingerloop activates cargo delivery and unloading during cotranslational protein targetingSecYEG activates GTPases to drive the completion of cotranslational protein targeting.A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel.Multiple conformational switches in a GTPase complex control co-translational protein targeting.Signal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.Fidelity of cotranslational protein targeting by the signal recognition particle.Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition ParticleSignal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Inhibitors of MAPK pathway ERK1/2 or p38 prevent the IL-1{beta}-induced up-regulation of SRP72 autoantigen in Jurkat cells.Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting.Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli.Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Sequential checkpoints govern substrate selection during cotranslational protein targeting.Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.The bacterial SRP receptor, FtsY, is activated on binding to the translocon.Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targetingThe Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
P2860
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P2860
Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Conformational changes in the ...... ation of protein translocation
@ast
Conformational changes in the ...... ation of protein translocation
@en
type
label
Conformational changes in the ...... ation of protein translocation
@ast
Conformational changes in the ...... ation of protein translocation
@en
prefLabel
Conformational changes in the ...... ation of protein translocation
@ast
Conformational changes in the ...... ation of protein translocation
@en
P2093
P2860
P356
P1476
Conformational changes in the ...... ation of protein translocation
@en
P2093
Peter Walter
Shu-ou Shan
Sowmya Chandrasekar
P2860
P304
P356
10.1083/JCB.200702018
P407
P577
2007-08-06T00:00:00Z