Multiple Distinct Assemblies Reveal Conformational Flexibility in the Small Heat Shock Protein Hsp26

Structure

Volumn 14, Issue 7, 2006, Pages 1197-1204

  White, Helen E ^a   Orlova, Elena V ^a   Chen, Shaoxia ^a   Wang, Luchun ^a   Ignatiou, Athanasios ^a   Gowen, Brent ^b   Stromer, Thusnelda ^c   Franzmann, Titus M ^c   Haslbeck, Martin ^c   Buchner, Johannes ^c   Saibil, Helen R ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; DIMER; HEAT SHOCK PROTEIN 26; PROTEIN SUBUNIT;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYOELECTRON MICROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MODIFICATION; YEAST;

ALPHA-CRYSTALLINS; BINDING SITES; CRYOELECTRON MICROSCOPY; DIMERIZATION; HEAT-SHOCK PROTEINS; PROTEIN STRUCTURE, QUATERNARY; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 33745855460     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.05.021     Document Type: Article

References (39)

1. Alexandrov N.N., Nussinov R., and Zimmer R.M. Fast protein fold recognition via sequence to structure alignment and contact capacity potentials. In: Hunter L., and Klein T.E. (Eds). Pacific Symposium on Biocomputing '96 (1995), World Scientific Publishing, Singapore 53-72
2. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
3. Bova M.P., Mchaourab H.S., Han Y., and Fung B.K.-K. Subunit exchange of small heat shock proteins: analysis of oligomeric formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J. Biol. Chem. 275 (2000) 1035-1042
4. Brady J.P., Garland D., Duglas-Tabor Y., Robison Jr. W.G., Groome A., and Wawrousek E.F. Targeted disruption of the mouse α-A crystallin genes induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein α-B crystallin. Proc. Natl. Acad. Sci. USA 94 (1997) 884-889
5. Cashikar A.G., Duennwald M., and Lindquist S.L. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 280 (2005) 23869-23875
6. Fischer D. Hybrid fold recognition: combining sequence derived properties with evolutionary information. Pacific Symp. Biocomputing, Hawaii (2000), World Scientific Publishing, Singapore 119-130
7. Franzmann T.M., Wuhr M., Richter K., Walter S., and Buchner J. The activation mechanism of Hsp26 does not require dissociation of the oligomer. J. Mol. Biol. 350 (2005) 1083-1093
8. Giese K.C., Basha E., Catague B.Y., and Vierling E. Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc. Natl. Acad. Sci. USA 102 (2005) 18896-18901
9. Haley D.A., Horwitz J., and Stewart P.L. The small heat-shock protein, αB-crystallin, has a variable quaternary structure. J. Mol. Biol. 277 (1998) 27-35
10. Haley D.A., Bova M.P., Huang Q.-L., Mchaourab H.S., and Stewart P.L. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J. Mol. Biol. 298 (2000) 261-272
11. Haslbeck M. sHsps and their role in the chaperone network. Cell. Mol. Life Sci. 59 (2002) 1649-1657
12. Haslbeck M., Walke S., Stromer T., Ehrnsperger M., White H.E., Chen S., Saibil H.R., and Buchner J. Hsp26: a temperature-regulated chaperone. EMBO J. 18 (1999) 6744-6751
13. Haslbeck M., Braun N., Stromer T., Richter B., Model N., Weikauf S., and Buchner J. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J. 23 (2004) 636-649
14. Haslbeck M., Ignatiou A., Saibil H.R., Helmich S., Franzl E., Stromer T., and Buchner J. A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J. Mol. Biol. 343 (2004) 445-455
15. Haslbeck M., Franzmann T., Weinfurtner D., and Buchner J. Some like it hot: the structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12 (2005) 842-846
16. Haslbeck M., Meiss A., Stromer T., Walter S., and Buchner J. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J. Biol. Chem. 280 (2005) 23861-23868
17. Horwitz J. Alpha-crystallin. Exp. Eye Res. 76 (2003) 145-153
18. Kappe G., Franck E., Verschuure P., Boelens W.C., Leunissen J.A., and de Jong W.W. The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 8 (2003) 53-61
19. Kelley L.A., MacCallum R.M., and Sternberg M.J.E. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299 (2000) 499-520
20. Kennaway C.K., Benesch J.L., Gohlke U., Wang L., Robinson C.V., Orlova E.V., Saibil H.R., and Keep N.H. Dodecameric structure of the small heat shock protein ACR1 from mycobacterium tuberculosis. J. Biol. Chem. 280 (2005) 33419-33425
21. Kim K.K., Kim R., and Kim S.-H. Crystal structure of a small heat shock protein. Nature 394 (1998) 595-599
22. Koteiche H.A., Chiu S., Majdoch R.L., Stewart P.L., and Mchaourab H.S. Atomic models by cryo-EM and site-directed spin labeling: application to the N-terminal region of Hsp16.5. Structure 13 (2005) 1165-1171
23. Lee G.L., Roseman A.M., Saibil H.R., and Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16 (1997) 659-671
24. Lee U., Wie C., Escobar M., Williams B., Hong S.-W., and Vierling E. Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. Plant Cell 17 (2005) 559-571
25. Mogk A., Deurling E., Vorderwülbecke S., Vierling E., and Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol. Microbiol. 50 (2003) 585-595
26. Narberhaus F. α-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66 (2002) 64-93
27. Navaza J., Lepault J., Rey F.A., Alvarez-Rua C., and Borge J. On the fitting of model electron densities into EM reconstructions: a reciprocal-space formulation. Acta Crystallogr. D Biol. Crystallogr. 58 (2000) 1820-1825
28. Pearson W.A. Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol. 183 (1990) 63-98
29. Roseman A.M. Docking structures of domains into maps from cryo-electron microscopy using local correlation. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1332-1340
30. Rost B., Yachdav G., and Liu J. The PredictProtein server. Nucleic Acids Res. 32 (2004) W321-W325
31. Shi J., Blundell T.L., and Mizuguchi K. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310 (2001) 243-257
32. Stamler R., Kappe G., Boelens W., and Slingsby C. Wrapping the α-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353 (2005) 68-79
33. Stromer T., Ehrnsperger M., Gaestel M., and Buchner J. Analysis of the interaction of small heat shock proteins with unfolding proteins. J. Biol. Chem. 278 (2003) 18015-18021
34. Stromer T., Fischer E., Richter K., Haslbeck M., and Buchner J. Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domain is important for oligomer assembly and the binding of unfolding proteins. J. Biol. Chem. 279 (2004) 11222-11228
35. van Heel M., Harauz G., Orlova E., Schmidt R., and Schatz M. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116 (1996) 17-24
36. van Montfort R.L.M., Basha E., Friedrich K.L., Slingsby C., and Vierling E. Crystal structure of a eukaryotic small heat shock protein. Nat. Struct. Biol. 8 (2001) 1025-1030
37. van Montfort R.L.M., Slingsby C., and Vierling E. Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. In: Horwich A. (Ed). Protein Folding in the Cell: Advances in Protein Structure Volume 59 (2002), Academic Press, San Diego 105-156
38. Veinger L., Diamant S., Buchner J., and Goloubinoff P. The small heat-shock protein ibpb from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273 (1998) 11032-11037
39. White H.E., Saibil H.R., Ignatiou A., and Orlova E.V. Recognition and separation of single particles with size variation by statistical analysis of their images. J. Mol. Biol. 336 (2004) 453-460