Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90.
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 alpha-lactalbumin to each other in an ATP-dependent manner. The two chaperones have additive effects in preventing rhodanese aggregation.
Schnaider
T
T
Department of Medical Chemistry, Semmelweis University, Budapest, Hungary.
Soti
C
C
Cheetham
M E
ME
Miyata
Y
Y
Yahara
I
I
Csermely
P
P
D050956:HSP40 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D007768:Lactalbumin / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D011485:Protein Binding
C121958:DNAJB2 protein, human; D050956:HSP40 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D007768:Lactalbumin