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Science 6 December 1996:
Vol. 274. no. 5293, pp. 1715 - 1717
DOI: 10.1126/science.274.5293.1715
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Reports

Chaperone Function of Hsp90-Associated Proteins

Suchira Bose, Tina Weikl, Hans Bügl, Johannes Buchner *

The Hsp90 heat shock protein of eukaryotic cells regulates the activity of proteins involved in signal transduction pathways and may direct intracellular protein folding in general. Hsp90 performs at least part of its function in a complex with a specific set of partner proteins that include members of the prolyl isomerase family. The properties of the major components of the Hsp90 complex were examined through the use of in vitro protein folding assays. Two of the components, FKBP52 and p23, functioned as mechanistically distinct molecular chaperones. These results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells.

Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, 93040 Regensburg, Germany.
*   To whom correspondence should be addressed. E-mail:johannes.buchner{at}biologie.uni-regensburg.de

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Biochemical and Genetic Characterization of an FK506-Sensitive Peptidyl Prolyl cis-trans Isomerase from a Thermophilic Archaeon, Methanococcus thermolithotrophicus.
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Y. Miyata, B. Chambraud, C. Radanyi, J. Leclerc, M.-C. Lebeau, J.-M. Renoir, R. Shirai, M.-G. Catelli, I. Yahara, and E.-E. Baulieu (1997)
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   Abstract »    Full Text »    PDF »
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H. J. Oh, X. Chen, and J. R. Subjeck (1997)
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   Abstract »    Full Text »    PDF »
In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.
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   Abstract »    Full Text »    PDF »
All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in cerevisiae.
K. Dolinski, S. Muir, M. Cardenas, and J. Heitman (1997)
PNAS 94, 13093-13098
   Abstract »    Full Text »    PDF »
Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides.
M. R. Leroux, R. Melki, B. Gordon, G. Batelier, and E. P. M. Candido (1997)
J. Biol. Chem. 272, 24646-24656
   Abstract »    Full Text »    PDF »
ATP-binding Properties of Human Hsp90.
T. Scheibel, S. Neuhofen, T. Weikl, C. Mayr, J. Reinstein, P. D. Vogel, and J. Buchner (1997)
J. Biol. Chem. 272, 18608-18613
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Molecular Characterization of a Small Heat Shock/alpha -Crystallin Protein in Encysted Artemia Embryos.
P. Liang, R. Amons, J. S. Clegg, and T. H. MacRae (1997)
J. Biol. Chem. 272, 19051-19058
   Abstract »    Full Text »    PDF »
Cdc37 is a molecular chaperone with specific functions in signal transduction..
Y Kimura, S L Rutherford, Y Miyata, I Yahara, B C Freeman, L Yue, R I Morimoto, and S Lindquist (1997)
Genes & Dev. 11, 1775-1785
   Abstract »    PDF »
Unique Structural Features of a Novel Class of Small Heat Shock Proteins.
M. R. Leroux, B. J. Ma, G. Batelier, R. Melki, and E. P. M. Candido (1997)
J. Biol. Chem. 272, 12847-12853
   Abstract »    Full Text »    PDF »
Nucleotides and Two Functional States of hsp90.
W. Sullivan, B. Stensgard, G. Caucutt, B. Bartha, N. McMahon, E. S. Alnemri, G. Litwack, and D. Toft (1997)
J. Biol. Chem. 272, 8007-8012
   Abstract »    Full Text »    PDF »
Molecular chaperones and the cytoskeleton.
P Liang and T. MacRae (1997)
J. Cell Sci. 110, 1431-1440
   Abstract »    PDF »
B-ind1, a Novel Mediator of Rac1 Signaling Cloned from Sodium Butyrate-treated Fibroblasts.
D. Courilleau, E. Chastre, M. Sabbah, G. Redeuilh, A. Atfi, and J. Mester (2000)
J. Biol. Chem. 275, 17344-17348
   Abstract »    Full Text »    PDF »
Overlapping Sites of Tetratricopeptide Repeat Protein Binding and Chaperone Activity in Heat Shock Protein 90.
A. J. Ramsey, L. C. Russell, S. R. Whitt, and M. Chinkers (2000)
J. Biol. Chem. 275, 17857-17862
   Abstract »    Full Text »    PDF »
Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone.
A. J. Weaver, W. P. Sullivan, S. J. Felts, B. A. L. Owen, and D. O. Toft (2000)
J. Biol. Chem. 275, 23045-23052
   Abstract »    Full Text »    PDF »
Hsp90 Chaperone Activity Requires the Full-length Protein and Interaction among Its Multiple Domains.
B. D. Johnson, A. Chadli, S. J. Felts, I. Bouhouche, M. G. Catelli, and D. O. Toft (2000)
J. Biol. Chem. 275, 32499-32507
   Abstract »    Full Text »    PDF »
Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins from Saccharomyces cerevisiae, Differ in Their Functional Properties.
C. Mayr, K. Richter, H. Lilie, and J. Buchner (2000)
J. Biol. Chem. 275, 34140-34146
   Abstract »    Full Text »    PDF »
Localization of the Chaperone Domain of FKBP52.
F. Pirkl, E. Fischer, S. Modrow, and J. Buchner (2001)
J. Biol. Chem. 276, 37034-37041
   Abstract »    Full Text »    PDF »
Stoichiometry, Abundance, and Functional Significance of the hsp90/hsp70-based Multiprotein Chaperone Machinery in Reticulocyte Lysate.
P. J. M. Murphy, K. C. Kanelakis, M. D. Galigniana, Y. Morishima, and W. B. Pratt (2001)
J. Biol. Chem. 276, 30092-30098
   Abstract »    Full Text »    PDF »
The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA. I. INCREASED FUNCTIONAL EXPRESSION OF ANTIBODY FRAGMENTS WITH AND WITHOUT cis-PROLINES.
H. Bothmann and A. Pluckthun (2000)
J. Biol. Chem. 275, 17100-17105
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The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA. II. ISOMERASE-INDEPENDENT CHAPERONE ACTIVITY IN VITRO.
K. Ramm and A. Pluckthun (2000)
J. Biol. Chem. 275, 17106-17113
   Abstract »    Full Text »    PDF »


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