Zuotin, a ribosome-associated DnaJ molecular chaperone

Wei Yan, Brenda Schilke, Christine Pfund, William Walter, Suwon Kim, Elizabeth A. Craig

Research output: Contribution to journalArticlepeer-review

140 Scopus citations


Correct folding of newly synthesized polypeptides is thought to be facilitated by Hsp70 molecular chaperones in conjunction with DnaJ cohort proteins. In Saccharomyces cerevisiae, SSB proteins are ribosome-associated Hsp70s which interact with the newly synthesized nascent polypeptide chain. Here we report that the phenotypes of an S.cerevisiae strain lacking the DnaJ-related protein Zuotin (Zuo1) are very similar to those of a strain lacking Ssb, including sensitivities to low temperatures, certain protein synthesis inhibitors and high osmolarity. Zuo1, which has been shown previously to be a nucleic acid-binding protein, is also a ribosome-associated protein localized predominantly in the cytosol. Analysis of zuo1 deletion and truncation mutants revealed a positive correlation between the ribosome association of Zuo1 and its ability to bind RNA. We propose that Zuo1 binds to ribosomes, in part, by interaction with ribosomal RNA and that Zuo1 functions with Ssb as a chaperone on the ribosome.

Original languageEnglish (US)
Pages (from-to)4809-4817
Number of pages9
JournalEMBO Journal
Issue number16
StatePublished - Aug 17 1998


  • DnaJ
  • Molecular chaperone
  • RNA binding
  • Ribosome
  • Zuo1

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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