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TranscriptomicsRNA coimmunoprecipitations
Nascent polypeptides emerging from the ribosome during biogenesis can interact with many chaperones and protein homeostasis factors. The high sensitivity of RNA identification can be used to identify substrates of specific cotranslationally acting chaperones. Protein A-tagged (TAP-tag) chaperones as...
ORGANISM(S): Saccharomyces cerevisiae 
2013-04-05 | E-GEOD-45794 | biostudies-arrayexpress
TranscriptomicsDefining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.
This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
ORGANISM(S): Saccharomyces cerevisiae 
2013-04-05 | E-GEOD-45798 | biostudies-arrayexpress
ProteomicsUnexpected role of a truncated ribosome-associated chloroplast trigger factor homolog serving ribosome biogenesis in plants - Data set 1 (Global proteome of wt and tig2 mutants)
Molecular chaperones are essential throughout a protein's life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typical trigger...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-12-09 | PXD057252 | Pride
Chaperone Arabidopsis 
UnknownStructural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone.
Not available
S-EPMC10539794 | biostudies-literature
TranscriptomicsSelective ribosome profiling reveals the co-translational chaperone action of trigger factor in vivo
As nascent polypeptides exit ribosomes, they are engaged by a series of processing, targeting and folding factors. Here we present a selective ribosome profiling strategy that enables global monitoring of when these factors engage polypeptides in the complex cellular environment. Studies of the Esch...
ORGANISM(S): Escherichia coli 
2011-12-09 | E-GEOD-33671 | biostudies-arrayexpress
ProteomicsMS data for Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis
Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. It is not clear how this promiscuous mechanism ensure efficient production of challenging clients such as highly expressed proteins. Here we find that the biogenesis of the abund...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-06-16 | PXD043391 | Pride
Ribosome-associated chaperone Hsf1 activation Eef1a biogenesis 
GenomicsNascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1
Nascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1
PRJNA635625 | ENA
GenomicsNascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1
Nascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1
PRJNA1424933 | ENA
UnknownThe ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.
Not available
S-EPMC10711665 | biostudies-literature
UnknownA ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex.
Not available
S-EPMC7673040 | biostudies-literature
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