Small heat shock protein AgsA forms dynamic fibrils

FEBS Letters

Volumn 585, Issue 21, 2011, Pages 3396-3402

  Shi, Xiaodong ^a   Wang, Zhao ^b   Yan, Linxuan ^a   Ezemaduka, Anastasia N ^a   Fan, Guizhen ^b   Wang, Rui ^c   Fu, Xinmiao ^a   Yin, Changcheng ^b   Chang, Zengyi ^a  

^a PEKING UNIVERSITY   (China)

^b PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

Amyloid; Chaperone; Cryo electron tomography; Electron microscopy; Fibril; Small heat shock protein

Indexed keywords

AGGREGATION SUPPRESSING PROTEIN; AMYLOID; BOVINE INSULIN; CHAPERONE; DITHIOTHREITOL; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN AGSA; OLIGOMER; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; COMPLEX FORMATION; CONTROLLED STUDY; DISSOCIATION; ELECTRON MICROSCOPY; FIBRIL FORMATION; HIGH TEMPERATURE; IN VITRO STUDY; LOW TEMPERATURE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; TEMPERATURE DEPENDENCE; TEMPERATURE SENSITIVITY;

BACTERIAL PROTEINS; DITHIOTHREITOL; HEAT-SHOCK PROTEINS, SMALL; INSULIN; MICROSCOPY, ELECTRON; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SALMONELLA ENTERICA; TEMPERATURE;

SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM;

EID: 80255129390     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.09.042     Document Type: Article

References (35)

1. M. Haslbeck, T. Franzmann, D. Weinfurtner, and J. Buchner Some like it hot: the structure and function of small heat-shock proteins Nat. Struct. Mol. Biol. 12 2005 842 846 (Pubitemid 41486706)
2. H. Nakamoto, and L. Vigh The small heat shock proteins and their clients Cell Mol. Life Sci. 64 2007 294 306 (Pubitemid 46440201)
3. G.J. Lee, A.M. Roseman, H.R. Saibil, and E. Vierling 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 (Pubitemid 27067794)
4. M. Ehrnsperger, S. Graber, M. Gaestel, and J. Buchner Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation EMBO J. 16 1997 221 229 (Pubitemid 27049380)
5. L. Veinger, S. Diamant, J. Buchner, and P. Goloubinoff 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 (Pubitemid 28204946)
6. G.J. Lee, and E. Vierling A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein Plant Physiol. 122 2000 189 198
7. K. Wang, and A. Spector Alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner Eur. J. Biochem. 267 2000 4705 4721
8. H. Yang, S. Huang, H. Dai, Y. Gong, C. Zheng, and Z. Chang The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surface at mild condition: conformation flexibility and molecular chaperone activity Protein Sci 8 1999 174 179 (Pubitemid 29035530)
9. T. Stromer, M. Ehrnsperger, M. Gaestel, and J. Buchner Analysis of the interaction of small heat shock proteins with unfolding proteins J. Biol. Chem. 278 2003 18015 18021 (Pubitemid 36799411)
10. R. Van Montfort, C. Slingsby, and E. Vierling Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones Adv. Protein Chem. 59 2002 105 156
11. L. Gu, A. Abulimiti, W. Li, and Z. Chang Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. J. Mol Biol 319 2002 517 526 (Pubitemid 34729476)
12. W. Jiao, M. Qian, P. Li, L. Zhao, and Z. Chang The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli J. Mol. Biol. 347 2005 871 884 (Pubitemid 40357925)
13. G. Kappe, J.A. Leunissen, and W.W. De Jong Evolution and diversity of prokaryotic small heat shock proteins Pro. Mol. Subcell. Biol. 28 2002 1 17
14. T. Tomoyasu, A. Takaya, T. Sasaki, T. Nagase, R. Kikuno, M. Morioka, and T. Yamamoto A new heat shock gene, AgsA, which encodes a small chaperone involved in suppressing protein aggregation in Salmonella enterica serovar Typhimurium J. Bacteriol. 185 2003 6331 6339 (Pubitemid 37305533)
15. T. Tomoyasu, A. Tabata, and H. Nagamune Investigation of the chaperone function of the small heat shock protein-AgsA BMC Biochemistry 11 2010 27
16. S. Meehan, Y. Berry, B. Luisi, C.M. Dobson, J.A. Carver, and C.M. MacPhee Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation J. Biol. Chem. 279 2004 3413 3419 (Pubitemid 38140578)
17. Y. Wang, X. Zhang, L. He, and C. Zeng Effect of amino acids on the formation and cytotoxicity of bovine insulin fibril Fourth Mil. Med. Univ. 29 2008 964 966
18. Q. Hu, B. Zhou, and Y. Liang Study of hen egg-white lysozyme fibrilization J. Biol. 26 2009 13 17
19. R. Diaz, W.J. Rice, and D.L. Stokes Fourier-Bessel reconstruction of helical assemblies Methods in Enzymology Vol. 482 2010 Academic Press Waltham, Massachusetts pp. 163-165
20. S.P. Jesper, B.A. Christian, and E.O. Daniel Amyloid structure-one but not the same: the many levels of fibrillar polymorphism FEBS J. 277 2010 4591 4601
21. C.C. Kitts, and D.A. Vanden Bout Near-field scanning optical microscopy measurements of fluorescent molecular probes binding to insulin amyloid fibrils J. Phys. Chem. B 113 2009 12090 12095
22. S.M. Kelly, and N.C. Price The use of circular dichroism in the investigation of protein structure and function Curr. Protein Pept. Sci. 1 2000 349 384
23. J.R. Shearstone, and F. Baneyx Biochemical characterization of the small heat shock protein IbpB from Escherichia coli J. Biol. Chem. 274 1999 9937 9945
24. K.K. Kim, R. Kim, and S.H. Kim Crystal structure of a small heat-shock protein Nature 394 1998 595 599 (Pubitemid 28366837)
25. R.L. Van Montfort, E. Basha, K.L. Friedrich, C. Slingsby, and E. Vierling Crystal structure and assembly of a eukaryotic small heat shock protein Nat. Struct. Biol. 8 2001 1025 1030 (Pubitemid 33101621)
26. R.A. Lindner, A. Kapur, M. Mariani, S.J. Titmuss, and J.A. Carver Structural alterations of alpha-crystallin during its chaperone action Eur. J. Biochem. 258 1998 170 183 (Pubitemid 28538323)
27. K.C. Giese, and E. Vierling Changes in the oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro J. Biol. Chem. 277 2002 46310 46318 (Pubitemid 35417625)
28. R. Shashidharamurthy, H.A. Koteiche, J. Dong, and H.S. Mchaourab Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oliomer is required for recognition and binding of destabilized T4 lysozyme J. Biol. Chem. 280 2005 5281 5289 (Pubitemid 40280001)
29. E. Ratajczak, J. Stroecka, M. Matuszewska, S. Zitkiewicz, D. Kuczynśka-Wisńik, E. Laskowska, and K. Liberek IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB FEBS Lett. 584 2010 2253 2257
30. K. Usui, N. Ishii, Y. Kawarabayasi, and M. Yohda Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 Protein Sci. 13 2004 134 144 (Pubitemid 38021148)
31. M. Fändrich, M. Schmidt, and N. Grigorieff Recent progress in understanding Alzheimer's β-amyloid structures Trends Biochem. Sci. 36 2011 338 345
32. C. Sachse, C. Xu, K. Wieligmann, S. Diekmann, N. Grigorieff, and M. Fändrich Quaternary structure of a mature amyloid fibril from Alzheimer's A beta (1-40) peptide J. Mol. Biol. 362 2006 347 354 (Pubitemid 44278847)
33. M. Schmidt, C. Sachse, W. Richter, C. Xu, M. Fändrich, and N. Grigorieff Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures Proc. Natl. Acad. Sci. USA 106 2009 19813 19818
34. C.S. Goldsbury, S. Wirtz, S.A. Müller, S. Sunderji, P. Wicki, U. Aebi, and P. Frey Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors J. Struct. Biol. 130 2000 217 231
35. J. Meinhardt, C. Sachse, P. Hortschansky, N. Grigorieff, and M. Fändrich Abeta (1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils J. Mol. Biol. 386 2009 869 877