Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90

Tamás Schnaider, Csaba Soti, Michael E. Cheetham, Yoshihiko Miyata, Ichiro Yahara, Péter Csermely

Research output: Contribution to journalArticle

17 Citations (Scopus)


The 90 kDa heat shock protein (Hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins. Both genetic and in vitro refolding experiments using reticulocyte lysate have suggested a functional interaction of Hsp90 with yeast human homologues of E. coli DnaJ. Here we present direct evidence using surface plasmon resonance that Hsp90 and the human DnaJ homologue, HSJ1b, bind to each other. We also show that Hsp90 and HSJ1b transfer α-lactalbumin to each other in an ATP-dependent manner. The two chaperones have additive effects in preventing rhodanese aggregation. (C) 2000 Elsevier Science Inc.

Original languageEnglish
Pages (from-to)1455-1465
Number of pages11
JournalLife Sciences
Issue number12
Publication statusPublished - Aug 11 2000



  • DnaJ
  • HSJ1b
  • Hsp90
  • Molecular chaperone
  • Rhodanese
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

Cite this