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

Tamás Schnaider, C. Söti, Michael E. Cheetham, Yoshihiko Miyata, Ichiro Yahara, P. Csermely

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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
Volume67
Issue number12
DOIs
Publication statusPublished - Aug 11 2000

Fingerprint

Thiosulfate Sulfurtransferase
HSP90 Heat-Shock Proteins
Lactalbumin
Molecular Chaperones
Surface plasmon resonance
Heat-Shock Proteins
Yeast
Escherichia coli
Agglomeration
Adenosine Triphosphate
Surface Plasmon Resonance
Reticulocytes
Proteins
Yeasts
Experiments

Keywords

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

ASJC Scopus subject areas

  • Pharmacology

Cite this

Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90. / Schnaider, Tamás; Söti, C.; Cheetham, Michael E.; Miyata, Yoshihiko; Yahara, Ichiro; Csermely, P.

In: Life Sciences, Vol. 67, No. 12, 11.08.2000, p. 1455-1465.

Research output: Contribution to journalArticle

Schnaider, Tamás ; Söti, C. ; Cheetham, Michael E. ; Miyata, Yoshihiko ; Yahara, Ichiro ; Csermely, P. / Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90. In: Life Sciences. 2000 ; Vol. 67, No. 12. pp. 1455-1465.
@article{3727e2a5d2c549fc9d5c69c3fc6c9876,
title = "Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90",
abstract = "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.",
keywords = "DnaJ, HSJ1b, Hsp90, Molecular chaperone, Rhodanese, Surface plasmon resonance",
author = "Tam{\'a}s Schnaider and C. S{\"o}ti and Cheetham, {Michael E.} and Yoshihiko Miyata and Ichiro Yahara and P. Csermely",
year = "2000",
month = "8",
day = "11",
doi = "10.1016/S0024-3205(00)00735-9",
language = "English",
volume = "67",
pages = "1455--1465",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "12",

}

TY - JOUR

T1 - Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90

AU - Schnaider, Tamás

AU - Söti, C.

AU - Cheetham, Michael E.

AU - Miyata, Yoshihiko

AU - Yahara, Ichiro

AU - Csermely, P.

PY - 2000/8/11

Y1 - 2000/8/11

N2 - 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.

AB - 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.

KW - DnaJ

KW - HSJ1b

KW - Hsp90

KW - Molecular chaperone

KW - Rhodanese

KW - Surface plasmon resonance

UR - http://www.scopus.com/inward/record.url?scp=0034637117&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034637117&partnerID=8YFLogxK

U2 - 10.1016/S0024-3205(00)00735-9

DO - 10.1016/S0024-3205(00)00735-9

M3 - Article

C2 - 10983842

AN - SCOPUS:0034637117

VL - 67

SP - 1455

EP - 1465

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 12

ER -