Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.
about
Molecular mechanism and structure of Trigger Factor bound to the translating ribosomeStructures of SRP54 and SRP19, the Two Proteins that Organize the Ribonucleic Core of the Signal Recognition Particle from Pyrococcus furiosusL25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.Study on the chaperone properties of conserved GTPasesPredominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.Cotranslational folding increases GFP folding yieldStreptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2.Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes.Trigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperoneSelective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes.The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy.Regulation by a chaperone improves substrate selectivity during cotranslational protein targetingTranslation elongation regulates substrate selection by the signal recognition particle.Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperoninsA little help from my friends: quality control of presecretory proteins in bacteriaUnraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.Coupling between codon usage, translation and protein export in Escherichia coli.Cryo-electron microscopy of ribosomal complexes in cotranslational folding, targeting, and translocation.Signal recognition particle: an essential protein-targeting machine.Fidelity of cotranslational protein targeting by the signal recognition particle.Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC.Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli.Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation.Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.Structure of the E. coli signal recognition particle bound to a translating ribosome.Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsYFunctional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function.Sequential checkpoints govern substrate selection during cotranslational protein targeting.Versatility of trigger factor interactions with ribosome-nascent chain complexes.The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation.Conformation of the signal recognition particle in ribosomal targeting complexes.Single-molecule dynamics of the molecular chaperone trigger factor in living cells.Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel.Cytosolic targeting factor AKR2A captures chloroplast outer membrane-localized client proteins at the ribosome during translation.Real-time observation of trigger factor function on translating ribosomes.Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms.The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
P2860
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P2860
Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
name
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@ast
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@en
Trigger factor binds to ribosome-signal-recognition particle
@nl
type
label
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@ast
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@en
Trigger factor binds to ribosome-signal-recognition particle
@nl
prefLabel
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@ast
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@en
Trigger factor binds to ribosome-signal-recognition particle
@nl
P2093
P2860
P50
P356
P1476
Trigger factor binds to riboso ...... y binding of the SRP receptor.
@en
P2093
Iwona Buskiewicz
Johannes Jöckel
Shan-Qing Gu
P2860
P304
P356
10.1073/PNAS.0402231101
P407
P577
2004-05-17T00:00:00Z