ArticleNature communications2021
Pathway of Hsp70 interactions at the ribosome.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70-Hsp110 chaperone system.The FEBS journal · 2026Review
- Nascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1.Molecular cell · 2026Article
- Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026Review
- The cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.Nature communications · 2026Article
- Specific branches of the proteostasis network regulate the toxicity associated with mistranslation.Nucleic acids research · 2025Article
- Association of the tomato co-chaperone geneHorticulture research · 2025Article
- A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A.Nature communications · 2025Article
- Mechanisms of multidrug resistance caused by an Ipi1 mutation in the fungal pathogen Candida glabrata.Nature communications · 2025Article
- Reduction of Ribosomal Expansion Segments in Yeast Species of the Magnusiomyces/Saprochaete Clade.Genome biology and evolution · 2024Article
- NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo.Nucleic acids research · 2024Article
- 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
- Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022Article
- Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes.Annual review of biomedical data science · 2022Review
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotes, an Hsp70 molecular chaperone triad assists folding of nascent chains emerging from the ribosome tunnel. In fungi, the triad consists of canonical Hsp70 Ssb, atypical Hsp70 Ssz1 and J-domain protein cochaperone Zuo1. Zuo1 binds the ribosome at the tunnel exit. Zuo1 also binds Ssz1, tethering it to the ribosome, while its J-domain stimulates Ssb's ATPase activity to drive efficient nascent chain interaction. But the function of Ssz1 and how Ssb engages at the ribosome are not well understood. Employing in vivo site-specific crosslinking, we found that Ssb(ATP) heterodimerizes with Ssz1. Ssb, in a manner consistent with the ADP conformation, also crosslinks to ribosomal proteins across the tunnel exit from Zuo1. These two modes of Hsp70 Ssb interaction at the ribosome suggest a functionally efficient interaction pathway: first, Ssb(ATP) with Ssz1, allowing optimal J-domain and nascent chain engagement; then, after ATP hydrolysis, Ssb(ADP) directly with the ribosome.
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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.