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TitleThe cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Page 961, Year 2026
Publish dateJan 16, 2026
AuthorsYing Zhang / Lorenz Grundmann / Leonie Vollmar / Julia Schimpf / Volker Hübscher / Mohd Areeb / Irina Grishkovskaya / Anna Moddemann / Kerstin Werner / Thorsten Hugel / David Haselbach / Sabine Rospert /
PubMed AbstractCoupling of ribosomal translation with cotranslational protein folding is essential for cellular homeostasis. In eukaryotes, Hsp70 and its J-domain cochaperone, the heterodimeric ribosome-associated ...Coupling of ribosomal translation with cotranslational protein folding is essential for cellular homeostasis. In eukaryotes, Hsp70 and its J-domain cochaperone, the heterodimeric ribosome-associated complex (RAC), are central to this process; however, mechanistic insights into the coordination of Hsp70 function with translation remain limited. Here, we present two cryo-EM structures of the ribosome-bound yeast Hsp70 Ssb, identifying Rpl25/uL23 as the ribosomal binding site and revealing its interaction with a model nascent chain. Together with detailed biochemical and mutational analyses, these structures enable us to delineate the intricate RAC-dependent cycle, which positions the substrate binding domain of Ssb-ATP close to the tunnel exit to receive nascent chains. This arrangement allows Ssb to undergo substantial conformational changes upon ATP hydrolysis without steric clashes with the ribosome, while the substrate binding domain of Ssb, now anchored by the tightly bound nascent chain, remains close to the tunnel exit.
External linksNat Commun / PubMed:41545346 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

53861

9r9p

EMDB-53861, PDB-9r9p:
Yeast 80S with nascent chain in complex with Ssb1-ADP in the S2 state
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsRIBOSOME / Hsp70 / nascent chain / 80S / Ssb

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