ArticleNature structural & molecular biology2017
Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex.
Article 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 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- The cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.Nature communications · 2026Article
- InAIMS microbiology · 2025Article
- 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
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- Transformation of Chaetomium thermophilum and Affinity Purification of Native Thermostable Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Pathway of Hsp70 interactions at the ribosome.Nature communications · 2021Article
- Identification and expression analysis of heat-shock proteins in wheat infected with powdery mildew and stripe rust.The plant genome · 2021Article
- A functional interaction between GRP78 and Zika virus E protein.Scientific reports · 2021Article
- The chaperone Hsp70 is a BH3 receptor activated by the pro-apoptotic Bim to stabilize anti-apoptotic clients.The Journal of biological chemistry · 2020Article
- The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb.Nature communications · 2020Article
- Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein science : a publication of the Protein Society · 2020Review
- Intracellular HSP70L1 inhibits human dendritic cell maturation by promoting suppressive H3K27me3 and H2AK119Ub1 histone modifications.Cellular & molecular immunology · 2020Article
- Chaperone Interactions at the Ribosome.Cold Spring Harbor perspectives in biology · 2019Review
- Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC.Nature structural & molecular biology · 2017Review
- Structural basis of HypK regulating N-terminal acetylation by the NatA complex.Nature communications · 2017Article
- J-domain proteins promote client relay from Hsp70 during tail-anchored membrane protein targeting.The Journal of biological chemistryArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cotranslational chaperones assist de novo folding of nascent polypeptides, prevent them from aggregating and modulate translation. The ribosome-associated complex (RAC) is unique in that the Hsp40 protein Zuo1 and the atypical Hsp70 chaperone Ssz1 form a stable heterodimer, which acts as a cochaperone for the Hsp70 chaperone Ssb. Here we present the structure of the Chaetomium thermophilum RAC core comprising Ssz1 and the Zuo1 N terminus. We show how the conserved allostery of Hsp70 proteins is abolished and this Hsp70-Hsp40 pair is molded into a functional unit. Zuo1 stabilizes Ssz1 in trans through interactions that in canonical Hsp70s occur in cis. Ssz1 is catalytically inert and cannot adopt the closed conformation, but the substrate binding domain β is completed by Zuo1. Our study offers insights into the coupling of a special Hsp70-Hsp40 pair, which evolved to link protein folding and translation.
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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.