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During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we exam...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-02-11 | PXD030626 | Pride
Co-translational assembly counteracts promiscuous interactions - addendum
The HSP90/R2TP quaternary chaperone assembles key cellular machines, including the three nuclear RNA polymerases and many non-coding RNPs. Here, we show that the R2TP binds many partners co-translationally. Remarkably, its co-translational interactome reveals many novel potential clients, and side-b...
ORGANISM(S): Homo sapiens (Human) 
2026-01-06 | PXD061298 | Pride
During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we exam...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-02-11 | PXD028413 | Pride
It is generally assumed that mRNAs undergoing translation are protected from decay. Here, we show that mRNAs are, in fact, co-translationally degraded. This is a widespread and conserved process affecting most genes, where 5′–3′ transcript degradation follows the last translating ribosome, producing...
ORGANISM(S): Schizosaccharomyces pombe 
Co-translational determination of quaternary structures in chaperone factories
Molecular chaperones assist in protein folding by interacting with nascent polypeptide chains (NCs) during translation, but whether the ribosome can sense chaperone defects and abort translation of misfolding NCs has not been explored. Here we used quantitative proteomics in E. coli to investigate t...
ORGANISM(S): Escherichia coli 
2022-12-09 | PXD025219 | Pride
Co-translational binding of importins to nascent proteins
Proteome-wide determinants of co-translational chaperone binding in bacteria
PELOTA and HBS1 suppress co-translational messenger RNA decay in Arabidopsis [GMUCT]
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