Nature communications, 2021-09, Vol.12 (1), p.5666-5666, Article 5666
2021
Details
- Autor(en) / Beteiligte
- Titel
- Pathway of Hsp70 interactions at the ribosome
- Ist Teil von
- Nature communications, 2021-09, Vol.12 (1), p.5666-5666, Article 5666
- Ort / Verlag
- England: Nature Publishing Group
- Erscheinungsjahr
- 2021
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2041-1723eISSN: 2041-1723DOI: 10.1038/s41467-021-25930-8Titel-ID: cdi_doaj_primary_oai_doaj_org_article_101d4b2643d04db4b8351919b8a8bf11
- Format
- –
- Schlagworte
- Adenosine diphosphate, Adenosine triphosphatase, Adenosine Triphosphate - metabolism, Antibodies, ATP, Binding sites, Biochemistry, Biophysics, Chain drives, Chains, Crosslinking, Eukaryotes, Folding, Fungi, HSP70 Heat-Shock Proteins - genetics, HSP70 Heat-Shock Proteins - isolation & purification, HSP70 Heat-Shock Proteins - metabolism, Hsp70 protein, Hydrolysis, Mass spectrometry, Molecular Chaperones - genetics, Molecular Chaperones - isolation & purification, Molecular Chaperones - metabolism, Molecular Docking Simulation, Polypeptides, Protein Domains - genetics, Protein Folding, Protein Multimerization, Proteins, Recombinant Proteins - genetics, Recombinant Proteins - isolation & purification, Recombinant Proteins - metabolism, Ribosomal proteins, Ribosomal Proteins - metabolism, Ribosomes - metabolism, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins - genetics, Saccharomyces cerevisiae Proteins - isolation & purification, Saccharomyces cerevisiae Proteins - metabolism, Scientific imaging, Tandem Mass Spectrometry, Tethering, Tunnels