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Article

The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain.

Proceedings of the National Academy of Sciences of the United States of America - 2 Apr 2002

Hundley Heather, Eisenman Helene, Walter William, Evans Tara, Hotokezaka Yuka, Wiedmann Martin, Craig Elizabeth

Abstract excerpt

Two proteins of the Hsp70 class (Ssb and Ssz1) and one of the J-type class (Zuo1) of molecular chaperones reside on the yeast ribosome, with Ssz1 forming a stable heterodimer with Zuo1. We designed experiments to address the roles of these two distantly related ribosome-associated Hsp70s and thei...

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Identifiers

PMID: 11929993
DOI: 10.1073/pnas.062048399
PMCID: PMC123626

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11929993-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain.PMID 11929993Read ↗

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Activation of pleiotropic drug resistance by the J-protein and Hsp70-related proteins, Zuo1 and Ssz1.Semantic proximity Read ↗

Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Semantic proximity Read ↗

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