title: Small heat shock proteins are molecular chaperones.
abstract: Small heat shock proteins (sHsp) with a molecular mass of 15-30 kDa are ubiquitous and conserved. Up to now their function has remained enigmatic. Increased expression under heat shock conditions and their protective effect on cell viability at elevated temperatures suggest that they may have a function in the formation or maintenance of the native conformation of cytosolic proteins. To test this hypothesis we studied the influence of murine Hsp25, human Hsp27, and bovine alpha-B-crystallin (an eye lens protein homologous to sHsps) on the unfolding and refolding of citrate synthase and alpha-glucosidase in vitro. Here we show that all sHsps investigated act as molecular chaperones in these folding reactions. At stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins. Furthermore, they promote the functional refolding of these proteins after urea denaturation similar to GroE and Hsp90. The interaction both with unfolding and refolding proteins seems to be ATP-independent.
authors.affiliation: Institut für Biophysik & Physikalische Biochemie, Universität Regensburg, Germany.
authors.forename: U
authors.initials: U
authors.lastname: Jakob
authors.forename: M
authors.initials: M
authors.lastname: Gaestel
authors.forename: K
authors.initials: K
authors.lastname: Engel
authors.forename: J
authors.initials: J
authors.lastname: Buchner
mesh_terms: D016475:3T3 Cells; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001426:Bacterial Proteins / Q000494:pharmacology; D002417:Cattle; D018835:Chaperonin 10; D018834:Chaperonin 60; D002950:Citrate (si)-Synthase / Q000737:chemistry* / Q000378:metabolism; D003459:Crystallins / Q000494:pharmacology; D004789:Enzyme Activation; D006360:Heat-Shock Proteins / Q000494:pharmacology*; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D051379:Mice; D008970:Molecular Weight; D011489:Protein Denaturation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000494:pharmacology; D014508:Urea; D000520:alpha-Glucosidases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D003459:Crystallins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; D000255:Adenosine Triphosphate; D014508:Urea; D002950:Citrate (si)-Synthase; D000520:alpha-Glucosidases