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Chaperone Function of Hsp90-Associated Proteins
Suchira Bose, Tina Weikl, Hans Bugl and Johannes Buchner
New Series, Vol. 274, No. 5293 (Dec. 6, 1996), pp. 1715-1717
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/2890953
Page Count: 3
You can always find the topics here!Topics: Aggregation, Eukaryotic cells, Protein folding, Antibodies, Heat shock proteins, Cytosol, Kinetics
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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.
Science © 1996 American Association for the Advancement of Science