SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting
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The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targetingStructures of the E. coli translating ribosome with SRP and its receptor and with the translocon.The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTPInteraction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particleStructural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptorStructural basis of signal-sequence recognition by the signal recognition particleThe Crystal Structure of the Signal Recognition Particle in Complex with Its ReceptorStructural basis for the molecular evolution of SRP-GTPase activation by proteinEvolution 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 OrganismsThe 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 mutansStructure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Use of synthetic signal sequences to explore the protein export machinery.Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Allosteric response and substrate sensitivity in peptide binding of the signal recognition particle.Protein targeting by the signal recognition particle.Fingerloop activates cargo delivery and unloading during cotranslational protein targetingCharacterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F' factorsA distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathwayMessenger RNA Turnover Processes in Escherichia coli, Bacillus subtilis, and Emerging Studies in Staphylococcus aureus.Cryo-electron microscopy of ribosomal complexes in cotranslational folding, targeting, and translocation.Signal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.Inhibitors of MAPK pathway ERK1/2 or p38 prevent the IL-1{beta}-induced up-regulation of SRP72 autoantigen in Jurkat cells.Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting.SIMIBI twins in protein targeting and localization.
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P2860
SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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name
SRP RNA provides the physiolog ...... ranslational protein targeting
@en
SRP RNA provides the physiolog ...... ranslational protein targeting
@nl
type
label
SRP RNA provides the physiolog ...... ranslational protein targeting
@en
SRP RNA provides the physiolog ...... ranslational protein targeting
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prefLabel
SRP RNA provides the physiolog ...... ranslational protein targeting
@en
SRP RNA provides the physiolog ...... ranslational protein targeting
@nl
P2860
P356
P1433
P1476
SRP RNA provides the physiolog ...... ranslational protein targeting
@en
P2093
Richard J Spanggord
P2860
P304
P356
10.1261/RNA.135407
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P577
2006-12-12T00:00:00Z