Mouse Hsp25, a small heat shock protein. The role of its C-terminal extension in oligomerization and chaperone action

European Journal of Biochemistry

Volumn 267, Issue 7, 2000, Pages 1923-1932

  Lindner, Robyn A ^a   Carver, John A ^a   Ehrnsperger, Monika ^b   Buchner, Johannes ^b   Esposito, Gennaro ^e   Behlke, Joachim ^c   Lutsch, Gudrun ^c   Kotlyarov, Alexey ^c   Gaestel, Matthias ^c,d  

^a UNIVERSITY OF WOLLONGONG   (Australia)

^b UNIVERSITY OF REGENSBURG   (Germany)

^c MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^d MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^e NONE

Author keywords

Flexibility; Hsp25; Molecular chaperone; Small heat shock protein; Spectroscopy

Indexed keywords

ALPHA LACTALBUMIN; CHAPERONE; DITHIOTHREITOL; HEAT SHOCK PROTEIN 25;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; HYDROPHOBICITY; NONHUMAN; OLIGOMERIZATION; PRECIPITATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE;

ANIMALS; BASE SEQUENCE; BIOPOLYMERS; CIRCULAR DICHROISM; DNA PRIMERS; HEAT; HEAT-SHOCK PROTEINS; MICE; MICROSCOPY, ELECTRON; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; NEOPLASM PROTEINS; PROTEIN CONFORMATION; ULTRACENTRIFUGATION;

MAMMALIA;

EID: 0034067386     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01188.x     Document Type: Article

References (40)

1. Boelens, W.C. & de Jong, W.W. (1995) α-Crystallins, versatile stress-proteins. Mol. Biol. Report 21, 75-80.
2. Ehrnsperger, M., Buchner, J. & Gaestel, M. (1997) Structure and function of small heat shock proteins. In Molecular Chaperones in the Life Cycle of Proteins, Structure, Function and Mode of Action (Fink, A.L. & Goto, Y., eds), pp. 533-575. Marcel Dekker, New York.
3. Carver, J.A., Aquilina, J.A., Cooper, P.G., Williams, G.A. & Truscott, R.J.W. (1994) Alpha-crystallin: molecular chaperone and protein surfactant. Biochim. Biophys. Acta 1204, 195-206.
4. Ehrnsperger, M., Gräber, S., Gaestel, M. & Buchner, J. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221-229.
5. Groenen, P.J.T.A., Merck, K.B., de Jong, W.W. & Bloemendal, H. (1994) Structure and modifications of the junior chaperone alpha-crystallin - from lens transparency to molecular pathology. Eur. J. Biochem. 225, 1-19.
6. Behlke, J., Lutsch, G., Gaestel, M. & Bielka, H. (1991) Supramolecular structure of the recombinant murine small heat shock protein hsp25. FEBS Lett. 288, 119-122.
7. Kim, K.K., Kim, R. & Kim, S.-H. (1998) Crystal structure of a small heat-shock protein. Nature 394, 595-599.
8. Brady, J.P., Garland, D., Duglas-Tabor, Y., Robison, W.G. Jr, Groome, A. & Wawrousek, E.F. (1997) Targeted disruption of the mouse alpha-A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha-B-crystallin. Proc. Natl Acad. Sci. USA 94, 884-889.
9. 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin. FEBS Lett. 311, 143-149.
10. 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. FEBS Lett. 369, 305-310.
11. Esposito, G., Viglino, P., Fogolari, F., Gaestel, M. & Carver, J.A. (1998) Selective NMR experiments on macromolecules - implementation and analysis of QUIET-NOESY. J. Magn. Reson. 132, 204-213.
12. Smulders, R.H.P.H., Carver, J.A., Lindner, R.A., van Boekel, M.A.M., Bloemendal, H. & de Jong, W.W. (1996) Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity. J. Biol. Chem. 271, 29060-29066.
13. Carver, J.A., Nicholls, K.A., Aquilina, J.A. & Truscott, R.J.W. (1996) Age-related changes in bovine α-crystallin and high-molecular-weight protein. Exp. Eye Res. 63, 639-647.
14. Carver, J.A., Guerreiro, N., Nicholls, K.A. & Truscott, R.J.W. (1995) On the interaction of α-crystallin with unfolded proteins. Biochim. Biophys. Acta 1252, 251-260.
15. Lindner, R.A., Kapur, A., Mariani, M., Titmuss, S. & Carver, J.A. (1998) Structural alterations of α-crystallin during its chaperone action. Eur. J. Biochem. 258, 170-183.
16. Slingsby, C. & Bateman, O.A. (1990) Rapid separation of bovine beta-crystallin subunits beta B1, beta B2, beta B3, beta A3 and beta A4. Exp. Eye Res. 51, 21-26.
17. Engel, K., Knauf, U. & Gaestel, M. (1991) Generation of antibodies against human hsp27 and murine hsp25 by immunization with a chimeric small heat shock protein. Biomed. Biochim. Acta 50, 1065-1071.
18. Buchner, J., Ehrnsperger, M., Gaestel, M. & Walke, S. (1998) Purification and characterization of small heat shock proteins. Methods Enzymol. 290, 339-349.
19. Farahbakhsh, Z.T., Huang, Q.L., Ding, L.L., Altenbach, C., Steinhoff, H.J., Horwitz, J. & Hubbell, W.L. (1995) Interaction of alpha-crystallin with spin-labeled peptides. Biochemistry 34, 509-516.
20. Manavalan, P. & Johnson, W.C. Jr (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 76-85.
21. Behlke, J., Ristau, O. & Schönfeld, H.-J. (1997) Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry 36, 5149-5156.
22. Behlke, J. & Ristau, O. (1997) Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72, 428-434.
23. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
24. Werten, P.J.L., Carver, J.A., Jaenicke, R. & de Jong, W.W. (1996) The elusive role of the N-terminal extension βA3- and βA1-crystallin. Prot. Eng. 9, 1021-1028.
25. Merck, K.B., Horwitz, J., Kersten, M., Overkamp, P., Gaestel, M., Bloemendal, H. & de Jong, W.W. (1993) Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein. Mol. Biol. Report 18, 209-215.
26. Kuwajima, K., Ikeguchi, M., Sugawara, T., Hiraoka, Y. & Sugai, S. (1990) Kinetics of disulfide bond reduction in alpha-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. Biochemistry 29, 8240-8249.
27. Lindner, R.A., Kapur, A. & Carver, J.A. (1997) The interaction of the molecular chaperone, α-crystallin, with molten globule states of bovine α-lactalbumin. J. Biol. Chem. 272, 27722-27729.
28. Zavialov, A., Benndorf, R., Ehrnsperger, M., Zav'yalov, V., Dudich, I., Buchner, J. & Gaestel, M. (1998) The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. Int. J. Biol. Macromol. 22, 163-173.
29. Das, K.P. & Surewicz, W.K. (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 369, 321-325.
30. Raman, B., Ramakrishna, T. & Rao, Ch.M. (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 365, 133-136.
31. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
32. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids. J. Wiley, New York.
33. 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbor effects. J. Biomol. NMR 5, 67-81.
34. Caspers, G.J., Leunissen, J.A.M. & de Jong, W.W. (1995) The expanding small heat-shock protein family, and structure predictions of the conserved alpha-crystallin domain. J. Mol. Evol. 40, 238-248.
35. Smulders, R.H.P.H., van Boekel, M.A. & de Jong, W.W. (1998) Mutations and modifications support a 'pitted-flexiball' model for α-crystallin. Int. J. Biol. Macromol. 22, 187-196.
36. van Boekel, M.A.M., Lange, F., de Grip, W.J. & de Jong, W.W. (1999) Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activity. Biochim. Biophys. Acta 1434, 114-123.
37. Lee, C.Y., McCammon, J.A. & Rossky, P.J. (1984) The structure of liquid water at an extended hydrophobic surface. J. Chem. Phys. 80, 4448-4455.
38. Leroux, M.R., Melki, R., Gordon, B., Batelier, G. & Candido, E.P.M. (1997) Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 272, 24646-24656.
39. Wistow, G. (1985) Domain structure and evolution in alpha-crystallins and small heat-shock proteins. FEBS Lett. 181, 1-6.
40. Siezen, R.J. & Hoenders, H.J. (1979) The quartemary structure of bovine alpha-crystallin. Surface probing by limited proteolysis in vitro. Eur. J. Biochem. 96, 431-440.