參考文獻 |
1. Ahner, A., Nakatsukasa, K., and Zhang, H. (2007). Small heat-shock proteins select ΔF508-CFTR for endoplasmic reticulum-associated degradation. Mol. Biol. 18, 806–814. doi:10.1091/mbc.E06.
2. Andreu, J. M., and Timasheff, S. N. (1986). The measurement of cooperative protein self-assembly by turbidity and other techniques. Methods Enzymol. 130, 47–59. doi:10.1016/0076-6879(86)30007-7.
3. Basha, E., Friedrich, K. L., and Vierling, E. (2006). The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity. J. Biol. Chem. 281, 39943–52. doi:10.1074/jbc.M607677200.
4. Basha, E., O’Neill, H., and Vierling, E. (2012). Small heat shock proteins and α-crystallins: Dynamic proteins with flexible functions. Trends Biochem. Sci. 37, 106–117. doi:10.1016/j.tibs.2011.11.005.
5. Biasini, M., Bienert, S., Waterhouse, A., Arnold, K., Studer, G., Schmidt, T., et al. (2014). SWISS-MODEL: Modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, 252–258. doi:10.1093/nar/gku340.
6. Bova, M. P., Mchaourab, H. S., Han, Y., and Fung, B. K.-K. (2000). Subunit Exchange of Small Heat Shock Proteins: Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J. Biol. Chem. 275, 1035–1042. doi:10.1074/jbc.275.2.1035.
7. de Jong, W. W., Caspers, G. J., and Leunissen, J. a (1998). Genealogy of the alpha-crystallin--small heat-shock protein superfamily. Int. J. Biol. Macromol. 22, 151–162. doi:10.1016/S0141-8130(98)00013-0.
8. de Rocher, A. E., and Vierling, E. (1994). Developmental control of small heat shock proteins expression during pea seed maturation. Plant J. 5, 93–102.
9. Ehrnsperger, M., Gräber, S., Gaestel, M., and Buchner, J. (1997). Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221–9. doi:10.1093/emboj/16.2.221.
10. Fleckenstein, T., Kastenmüller, A., Stein, M. L., Peters, C., Daake, M., Krause, M., et al. (2015). The chaperone activity of the developmental small heat shock protein Sip1 is regulated by pH-dependent conformational changes. Mol. Cell 58, 1067–1078. doi:10.1016/j.molcel.2015.04.019.
11. Giese, K. C., Basha, E., Catague, B. Y., and Vierling, E. (2005). 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. U. S. A. 102, 18896–901. doi:10.1073/pnas.0506169103.
12. Haley, D. a, Horwitz, J., and Stewart, P. L. (1998). The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. J. Mol. Biol. 277, 27–35. doi:10.1006/jmbi.1997.1611.
13. Hanazono, Y., Takeda, K., Oka, T., Abe, T., Tomonari, T., Akiyama, N., et al. (2013). Nonequivalence observed for the 16-meric structure of a small heat shock protein, SpHsp16.0, from Schizosaccharomyces pombe. Structure 21, 220–228. doi:10.1016/j.str.2012.11.015.
14. Hanazono, Y., Takeda, K., Yohda, M., and Miki, K. (2012). Structural studies on the oligomeric transition of a small heat shock protein, StHsp14.0. J. Mol. Biol. 422, 100–108. doi:10.1016/j.jmb.2012.05.017.
15. Haslbeck, M., Franzmann, T., Weinfurtner, D., and Buchner, J. (2005). Some like it hot: the structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12, 842–6. doi:10.1038/nsmb993.
16. Hilario, E., Martin, F. J. M., Bertolini, M. C., and Fan, L. (2011). Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer. J. Mol. Biol. 408, 74–86. doi:10.1016/j.jmb.2011.02.004.
17. Jehle, S., Vollmar, B. S., Bardiaux, B., Dove, K. K., Rajagopal, P., Gonen, T., et al. (2011). N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc. Natl. Acad. Sci. U. S. A. 108, 6409–6414. doi:10.1073/pnas.1014656108.
18. Kennaway, C. K., Benesch, J. L. P., Gohlke, U., Wang, L., Robinson, C. V, Orlova, E. V, et al. (2005). Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis. J. Biol. Chem. 280, 33419–25. doi:10.1074/jbc.M504263200.
19. Kim, K. K., Kim, R., and Kim, S. H. (1998). Crystal structure of a small heat-shock protein. Nature 394, 595–9. doi:10.1038/29106.
20. Koteiche, H. a, Chiu, S., Majdoch, R. L., Stewart, P. L., and Mchaourab, H. S. (2005). Atomic models by cryo-EM and site-directed spin labeling: application to the N-terminal region of Hsp16.5. Structure 13, 1165–71. doi:10.1016/j.str.2005.05.006.
21. Koteiche, H. a, and Mchaourab, H. S. (2002). The determinants of the oligomeric structure in Hsp16.5 are encoded in the alpha-crystallin domain. FEBS Lett. 519, 16–22.
22. Lambert, H., Charette, S. J., Bernier, F., Guimond, A., and Landry, J. (1999). HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J. Biol. Chem. 274, 9378–9385.
23. Lambert, W., Koeck, P. J. B., Ahrman, E., Purhonen, P., Cheng, K., Elmlund, D., et al. (2011). Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21. Protein Sci. 20, 291–301. doi:10.1002/pro.560.
24. Lee, G. J., Roseman, a M., Saibil, H. R., and Vierling, E. (1997). A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16, 659–71. doi:10.1093/emboj/16.3.659.
25. Lepault, J., and Dubochet, J. (1986). Electron microscopy of frozen hydrated specimens: Preparation and characteristics. Methods Enzymol. 127, 719–730. doi:10.1016/0076-6879(86)27056-1.
26. Leroux, M. R., Melki, R., Gordon, B., Batelier, G., and Candido, E. P. (1997). Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 272, 24646–56. Available at: http://www.ncbi.nlm.nih.gov/pubmed/9305934.
27. Hsieh, M. H., Chen, J. T., Jinn, T. L., Chen, Y. M., and Lin, C. Y. (1992). A class of soybean low molecular weight heat shock proteins: immunological study and quantitation. Plant Physiol. 99, 1279–1284.
28. Moody, T. P., Donovan, M. A., and Laue, T. M. (1996). Turbidimetric studies of Limulus coagulin gel formation. Biophys. J. 71, 2012–2021. doi:10.1016/S0006-3495(96)79399-2.
29. Moutaoufik, M. T., Morrow, G., Finet, S., and Tanguay, R. M. (2017). Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure. PLoS One 12, e0177821. doi:10.1371/journal.pone.0177821.
30. Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., et al. (2004). UCSF Chimera—A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612. doi:10.1002/jcc.20084.
31. Rutsdottir, G., Härmark, J., Weide, Y., Hebert, H., Rasmussen, M. I., Wernersson, S., et al. (2017). Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity. J. Biol. Chem. 292, 8103–8121. doi:10.1074/jbc.M116.766816.
32. Stamler, R., Kappé, G., Boelens, W., and Slingsby, C. (2005). Wrapping the α-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353, 68–79. doi:10.1016/j.jmb.2005.08.025.
33. Stengel, F., Baldwin, A. J., Painter, A. J., Jaya, N., Basha, E., Kay, L. E., et al. (2010). Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proc. Natl. Acad. Sci. 107, 2007–2012. doi:10.1073/pnas.0910126107.
34. Studer, S., Obrist, M., Lentze, N., and Narberhaus, F. (2002). A critical motif for oligomerization and chaperone activity of bacterial α-heat shock proteins. Eur. J. Biochem. 269, 3578–3586. doi:10.1046/j.1432-1033.2002.03049.x.
35. Sung, D. Y., Kaplan, F., Lee, K. J., and Guy, C. L. (2003). Acquired tolerance to temperature extremes. Trends Plant Sci. 8, 179–187. doi:10.1016/S1360-1385(03)00047-5.
36. Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., et al. (2007). EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38–46. doi:10.1016/j.jsb.2006.05.009.
37. Thériault, J. R., Lambert, H., Chávez-Zobel, A. T., Charest, G., Lavigne, P., and Landry, J. (2004). Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J. Biol. Chem. 279, 23463–71. doi:10.1074/jbc.M402325200.
38. van Montfort, R. L., Basha, E., Friedrich, K. L., Slingsby, C., and Vierling, E. (2001). Crystal structure and assembly of a eukaryotic small heat shock protein. Nat. Struct. Biol. 8, 1025–30. doi:10.1038/nsb722.
39. Vierling, E. (1991). The roles of heat shock proteins in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 42, 579–620. doi:10.1146/annurev.pp.42.060191.003051.
40. Waters, E. R., Lee, G. J., and Vierling, E. (1996). Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47, 325–338. doi:10.1093/jxb/47.3.325.
41. White, H. E., Orlova, E. V, Chen, S., Wang, L., Ignatiou, A., Gowen, B., et al. (2006). Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure 14, 1197–204. doi:10.1016/j.str.2006.05.021.
42. Yeh, C. H., Yeh, K. W., Wu, S. H., Chang, P. F., Chen, Y. M., and Lin, C. Y. (1995). A recombinant rice 16.9-kDa heat shock protein can provide thermoprotection in vitro. Plant Cell Physiol. 36, 1341–1348.
43. Yeh, C. H., Chang, P. F., Yeh, K. W., Lin, W. C., Chen, Y. M., and Lin, C. Y. (1997). Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc. Natl. Acad. Sci. U. S. A. 94, 10967–72. doi:10.1073/pnas.94.20.10967. |