ArticlePLoS biology2011
Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.
Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed, 166 citations in OpenAlex.
- Article
- Co-translational protein targeting to mitochondria in the context of co-translational protein maturation.Protein science : a publication of the Protein Society · 2026Review
- SRP orchestrates protein biogenesis beyond initial ER membrane targeting.Nature communications · 2026Article
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- NAC promotes co-translational protein folding at the ribosomal tunnel exit.Molecular cell · 2026Article
- Article
- A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.Nature communications · 2026Article
- NAC couples protein synthesis with nascent polypeptide myristoylation on the ribosome.The EMBO journal · 2025Article
- Polyamine Induction of Secondary Metabolite Biosynthetic Genes in Fungi Is Mediated by Global Regulator LaeA and α-NAC Transcriptional Coactivator: Connection to Epigenetic Modification of Histones.Molecules (Basel, Switzerland) · 2025Review
- Ribosome biogenesis in plants requires the nuclear envelope and mitochondria localized OPENER complex.Nature communications · 2025Article
- Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.Nature communications · 2024Article
- Disruption of the nascent polypeptide-associated complex leads to reduced polyglutamine aggregation and toxicity.PloS one · 2024Article
- Quantification of elongation stalls and impact on gene expression in yeast.RNA (New York, N.Y.) · 2023Article
- The unfolded protein response of the endoplasmic reticulum supports mitochondrial biogenesis by buffering nonimported proteins.Molecular biology of the cell · 2023Article
- Control of mRNA fate by its encoded nascent polypeptide.Molecular cell · 2023Review
- Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein import.PLoS genetics · 2023Article
- Not4-dependent targeting of MMF1 mRNA to mitochondria limits its expression via ribosome pausing, Egd1 ubiquitination, Caf130, no-go-decay and autophagy.Nucleic acids research · 2023Article
- Quantification of elongation stalls and impact on gene expression in yeast.bioRxiv : the preprint server for biology · 2023Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- The nascent polypeptide-associated complex (NAC) controls translation initiation in cis by recruiting nucleolin to the encoding mRNA.Nucleic acids research · 2022Article
30 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Polypeptides exiting the ribosome must fold and assemble in the crowded environment of the cell. Chaperones and other protein homeostasis factors interact with newly translated polypeptides to facilitate their folding and correct localization. Despite the extensive efforts, little is known about the specificity of the chaperones and other factors that bind nascent polypeptides. To address this question we present an approach that systematically identifies cotranslational chaperone substrates through the mRNAs associated with ribosome-nascent chain-chaperone complexes. We here focused on two Saccharomyces cerevisiae chaperones: the Signal Recognition Particle (SRP), which acts cotranslationally to target proteins to the ER, and the Nascent chain Associated Complex (NAC), whose function has been elusive. Our results provide new insights into SRP selectivity and reveal that NAC is a general cotranslational chaperone. We found surprising differential substrate specificity for the three subunits of NAC, which appear to recognize distinct features within nascent chains. Our results also revealed a partial overlap between the sets of nascent polypeptides that interact with NAC and SRP, respectively, and showed that NAC modulates SRP specificity and fidelity in vivo. These findings give us new insight into the dynamic interplay of chaperones acting on nascent chains. The strategy we used should be generally applicable to mapping the specificity, interplay, and dynamics of the cotranslational protein homeostasis network.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.