Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.
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Molecular mechanism and structure of Trigger Factor bound to the translating ribosomePromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneStructural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26Structural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneTranscriptomic profiling of the oyster pathogen Vibrio splendidus opens a window on the evolutionary dynamics of the small RNA repertoire in the Vibrio genusSelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoRotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase.Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone actionMolecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.A little gene with big effects: a serT mutant is defective in flgM gene translation.A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains.Hydrophobic collapse of trigger factor monomer in solutionTrigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperoneRegulation by a chaperone improves substrate selectivity during cotranslational protein targetingBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Chaperone-assisted folding of newly synthesized proteins in the cytosol.Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperonesCalcineurin regulation in fungi and beyondIntegrating protein homeostasis strategies in prokaryotes.Breaking on through to the other side: protein export through the bacterial Sec system.Identification of nascent chain interaction sites on trigger factor.Versatility of trigger factor interactions with ribosome-nascent chain complexes.Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding.Granzyme B Disrupts Central Metabolism and Protein Synthesis in Bacteria to Promote an Immune Cell Death Program.Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures.Real-time observation of trigger factor function on translating ribosomes.The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.Trigger factor forms a protective shield for nascent polypeptides at the ribosome.Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli.Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.
P2860
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P2860
Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.
description
2004 nî lūn-bûn
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name
Functional dissection of Esche ...... unction of individual domains.
@en
type
label
Functional dissection of Esche ...... unction of individual domains.
@en
prefLabel
Functional dissection of Esche ...... unction of individual domains.
@en
P2093
P2860
P1476
Functional dissection of Esche ...... unction of individual domains.
@en
P2093
Deuerling E
Rutkowska A
Vorderwülbecke S
Wegrzyn RD
P2860
P304
P356
10.1128/JB.186.12.3777-3784.2004
P577
2004-06-01T00:00:00Z