Hsp26: a temperature-regulated chaperone - PubMed (original) (raw)
Hsp26: a temperature-regulated chaperone
M Haslbeck et al. EMBO J. 1999.
Abstract
Small heat shock proteins (sHsps) are a conserved protein family, with members found in all organisms analysed so far. Several sHsps have been shown to exhibit chaperone activity and protect proteins from irreversible aggregation in vitro. Here we show that Hsp26, an sHsp from Saccharomyces cerevisiae, is a temperature-regulated molecular chaperone. Like other sHsps, Hsp26 forms large oligomeric complexes. At heat shock temperatures, however, the 24mer chaperone complex dissociates. Interestingly, chaperone assays performed at different temperatures show that the dissociation of the Hsp26 complex at heat shock temperatures is a prerequisite for efficient chaperone activity. Binding of non-native proteins to dissociated Hsp26 produces large globular assemblies with a structure that appears to be completely reorganized relative to the original Hsp26 oligomers. In this complex one monomer of substrate is bound per Hsp26 dimer. The temperature-dependent dissociation of the large storage form of Hsp26 into a smaller, active species and the subsequent re-association to a defined large chaperone-substrate complex represents a novel mechanism for the functional activation of a molecular chaperone.
Similar articles
- The activation mechanism of Hsp26 does not require dissociation of the oligomer.
Franzmann TM, Wühr M, Richter K, Walter S, Buchner J. Franzmann TM, et al. J Mol Biol. 2005 Jul 29;350(5):1083-93. doi: 10.1016/j.jmb.2005.05.034. J Mol Biol. 2005. PMID: 15967461 - A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization.
Haslbeck M, Ignatiou A, Saibil H, Helmich S, Frenzl E, Stromer T, Buchner J. Haslbeck M, et al. J Mol Biol. 2004 Oct 15;343(2):445-55. doi: 10.1016/j.jmb.2004.08.048. J Mol Biol. 2004. PMID: 15451672 - Beyond transcription--new mechanisms for the regulation of molecular chaperones.
Winter J, Jakob U. Winter J, et al. Crit Rev Biochem Mol Biol. 2004 Sep-Dec;39(5-6):297-317. doi: 10.1080/10409230490900658. Crit Rev Biochem Mol Biol. 2004. PMID: 15763707 Review. - Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?
Carver JA, Rekas A, Thorn DC, Wilson MR. Carver JA, et al. IUBMB Life. 2003 Dec;55(12):661-8. doi: 10.1080/15216540310001640498. IUBMB Life. 2003. PMID: 14769002 Review.
Cited by
- Minimum information guidelines for experiments structurally characterizing intrinsically disordered protein regions.
Mészáros B, Hatos A, Palopoli N, Quaglia F, Salladini E, Van Roey K, Arthanari H, Dosztányi Z, Felli IC, Fischer PD, Hoch JC, Jeffries CM, Longhi S, Maiani E, Orchard S, Pancsa R, Papaleo E, Pierattelli R, Piovesan D, Pritisanac I, Tenorio L, Viennet T, Tompa P, Vranken W, Tosatto SCE, Davey NE. Mészáros B, et al. Nat Methods. 2023 Sep;20(9):1291-1303. doi: 10.1038/s41592-023-01915-x. Epub 2023 Jul 3. Nat Methods. 2023. PMID: 37400558 Review. - Breaking spore dormancy in budding yeast transforms the cytoplasm and the solubility of the proteome.
Plante S, Moon KM, Lemieux P, Foster LJ, Landry CR. Plante S, et al. PLoS Biol. 2023 Apr 20;21(4):e3002042. doi: 10.1371/journal.pbio.3002042. eCollection 2023 Apr. PLoS Biol. 2023. PMID: 37079504 Free PMC article. - Development of a Vector Set for High or Inducible Gene Expression and Protein Secretion in the Yeast Genus Blastobotrys.
Boisramé A, Neuvéglise C. Boisramé A, et al. J Fungi (Basel). 2022 Apr 19;8(5):418. doi: 10.3390/jof8050418. J Fungi (Basel). 2022. PMID: 35628674 Free PMC article. - The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin.
Li H, Yu Y, Ruan M, Jiao F, Chen H, Gao J, Weng Y, Bao Y. Li H, et al. Biophys J. 2022 Jun 21;121(12):2233-2250. doi: 10.1016/j.bpj.2022.05.032. Epub 2022 May 26. Biophys J. 2022. PMID: 35619565 Free PMC article. - Fungal communities represent the majority of root-specific transcripts in the transcriptomes of Agave plants grown in semiarid regions.
Marone MP, Campanari MFZ, Raya FT, Pereira GAG, Carazzolle MF. Marone MP, et al. PeerJ. 2022 May 2;10:e13252. doi: 10.7717/peerj.13252. eCollection 2022. PeerJ. 2022. PMID: 35529479 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases