ReviewNature structural & molecular biology2017
Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC.
Review in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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Who cites it
40 citing papers in PubMed, 61 citations in OpenAlex.
- Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1.Nucleic acids research · 2026Article
- The cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.Nature communications · 2026Article
- HYPK promotes N-terminal protein acetylation through rapid ribosome exchange of NatA.Molecular cell · 2025Article
- Circadian clock control of ribosome composition promotes rhythmic translation and termination fidelity.Cell reports · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- InAIMS microbiology · 2025Article
- NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo.Nucleic acids research · 2024Article
- The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways.Frontiers in molecular biosciences · 2024Review
- The ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.The EMBO journal · 2023Article
- Structural inventory of cotranslational protein folding by the eukaryotic RAC complex.Nature structural & molecular biology · 2023Article
- Exploration of the truncated cytosolic Hsp70 in plants - unveiling the diverse T1 lineage and the conserved T2 lineage.Frontiers in plant science · 2023Article
- Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation.Nucleic acids research · 2022Article
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- Article
- Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.Frontiers in molecular biosciences · 2022Review
- Pathway of Hsp70 interactions at the ribosome.Nature communications · 2021Article
- Selective functional inhibition of a tumor-derived p53 mutant by cytosolic chaperones identified using split-YFP in budding yeast.G3 (Bethesda, Md.) · 2021Article
- A role for the ribosome-associated complex in activation of the IRE1 branch of UPR.Cell reports · 2021Article
- Identification of protein quality control regulators using a Drosophila model of TPI deficiency.Neurobiology of disease · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperones, which assist protein folding are essential components of every living cell. The yeast ribosome-associated complex (RAC) is a chaperone that is highly conserved in eukaryotic cells. The RAC consists of the J protein Zuo1 and the unconventional Hsp70 homolog Ssz1. The RAC heterodimer stimulates the ATPase activity of the ribosome-bound Hsp70 homolog Ssb, which interacts with nascent polypeptide chains to facilitate de novo protein folding. In addition, the RAC-Ssb system is required to maintain the fidelity of protein translation. Recent work reveals important details of the unique structures of RAC and Ssb and identifies how the chaperones interact with the ribosome. The new findings start to uncover how the exceptional chaperone triad cooperates in protein folding and maintenance of translational fidelity and its connection to extraribosomal functions.
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What OpenQuestion holds
Registered trials
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.