Pathway of Hsp70 interactions at the ribosome
| Autor: | Thomas Ziegelhoffer, Grzegorz Sabat, Scott E Berger, Wojciech Delewski, Elizabeth A. Craig, Kanghyun Lee |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
musculoskeletal diseases
Ribosomal Proteins Protein Folding Saccharomyces cerevisiae Proteins Science General Physics and Astronomy Saccharomyces cerevisiae Ribosome General Biochemistry Genetics and Molecular Biology Article Adenosine Triphosphate stomatognathic system Protein Domains ATP hydrolysis Ribosomal protein Tandem Mass Spectrometry Chaperones Atpase activity HSP70 Heat-Shock Proteins skin and connective tissue diseases Multidisciplinary Chemistry Hydrolysis General Chemistry eye diseases Recombinant Proteins Hsp70 Folding (chemistry) Molecular Docking Simulation stomatognathic diseases Biophysics Protein Multimerization Ribosomes Function (biology) Molecular Chaperones |
| Zdroj: | Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. Here, the authors use in vivo site-specific crosslinking to provide molecular-level insight into how the fungal Hsp70 chaperone system — the Ssb:Ssz1:Zuo1 triad — assists the folding process for the nascent peptide chain emerging from the ribosome tunnel. |
| Databáze: | OpenAIRE |
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