Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 4, 2006, Pages 677-687

  Spinozzi, Francesco ^a   Mariani, Paolo ^a   Rustichelli, Franco ^a   Amenitsch, Heinz ^b   Bennardini, Federico ^c   Mura, Giovanni Maria ^c   Coi, Alessio ^c   Ganadu, Maria Luisa ^c  

^a UNIVERSITÀ POLITECNICA DELLE MARCHE   (Italy)

^b ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

^c UNIVERSITY OF SASSARI   (Italy)

Author keywords

B crystallin; Chaperone activity; Heat shock protein; Protein aggregation; Quaternary structure; SAXS

Indexed keywords

ALPHA CRYSTALLIN; INSULIN; OLIGOMER; THIOCYANATE; UREA;

ARTICLE; BETA CHAIN; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; TEMPERATURE DEPENDENCE;

ALPHA-CRYSTALLIN B CHAIN; DIMERIZATION; HEAT-SHOCK PROTEINS; HUMANS; INSULIN; MOLECULAR CHAPERONES; PLANT PROTEINS; PROTEIN STRUCTURE, QUATERNARY; TEMPERATURE; THIOCYANATES; UREA;

EID: 33646098185     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.02.003     Document Type: Article

References (47)

1. Derham B., and Harding J. α-crystallin as a molecular chaperone. Prog. Retin. Eye Res. 18 (1999) 463-509
2. Chiesi M., Longoni S., and Limbruno U. Cardiac α-crystallin: III. Involvement during heart ischemia. Mol. Cell. Biochem. 97 (1990) 129-136
3. Srinivasan A., Nagieni C., and Bhat S. αA-crystallin is expressed in non-ocular tissues. J. Biol. Chem. 267 (1992) 23337-23341
4. Veretout F., Delaye M., and Tardieu A. Molecular basis of eye lens transparency. osmotic pressure and X-ray analysis of alpha-crystallin solutions. J. Mol. Biol. 205 (1989) 713-728
5. Jakob U., Gaestel M., Engel K., and Buchner J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268 (1993) 1517-1520
6. Haslbeck M., and Buchner J. Small Stress Proteins (2002), Springer, Berlin
7. Kato K., Ito H., Inaguma Y., Okamoto K., and Saga S. Synthesis and accumulation of αB crystallin in C6 glioma cells is induced by agents that promote the disassembly of microtubules. J. Biol. Chem. 271 (1996) 26989-26994
8. Bennardini F., Wrzosek A., and Chiesi M. αB-crystallin in cardiac tissue. association with actin and desmin filaments. Circ. Res. 71 (1992) 288-294
9. Vicart P., Caron A., Guicheney P., Li Z., Prevost M., Faure A., Chateau D., Chapon F., Tome F., Dupret J., Paulin D., and Fardeau M. A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20 (1998) 92-95
10. Ehrnsperger M., Gräber S., Gaestel M., and Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16 (1997) 221-229
11. Lee G.J., Roseman H.R.S.A.M., 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
12. Horwitz J., Huang Q., Ding L., and Bova M. Lens α-crystallin: chaperone-like properties. Methods Enzymol. 290 (1998) 365-383
13. Bettelheim F., Ansari R., Cheng Q., and Zigler J. The mode of chaperoning of dithiothreitol-denatured α-lactalbumin by α-crystallin. Biochem. Biophys. Res. Commun. 261 (1999) 292-297
14. Lindner R., Kapur A., Mariani M., Titmuss J., and Carver J. Structural alterations of α-crystallin during its chaperone action. Eur. J. Biochem. 258 (1998) 170-183
15. van de Klundert F., Gysen R., Lindner M., Jaenicke R., Carver J., and de Jong W. The mammalian small heat-shock protein hsp20 forms dimers and is a poor chaperone. Eur. J. Biochem. 258 (1998) 1014-1021
16. Bhattacharyya J., and Das K. α-crystallin does not require temperature activation for its chaperone-like activity. Mol. Biol. Int. 6 (1998) 249-258
17. Das K., and Surewicz W. Temperature induced exposure of hydrophobic surfaces and its effect on chaperone activity of α-crystallin. FEBS Lett. 369 (1995) 321-325
18. Raman B., Ramakrishna T., and Rao C. Temperature dependent chaperone-like activity of α-crystallin. FEBS Lett. 365 (1995) 133-136
19. Horwitz J. α-crystallin. Exp. Eye. Res. 76 (2003) 145-153
20. Crabbe M., and Goode D. Protein folds and functional similarity; the Greek key/immunoglobulin fold. Comput. Commer. 19 (1995) 343-349
21. Kim K., Kim R., and Kim S. Crystal structure of a small heat-shock protein. Nature 394 (1998) 595-599
22. Kim R., Kim K., Yokota H., and Kim S. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. Proc. Natl. Acad. Sci. 95 (1998) 9129-9133
23. Haley D.A., Horwitz J., and Stewart P.L. Image restrained modeling of αB-crystallin. Exp. Eye Res. 68 (1999) 133-136
24. Groenen P.J., Merck K.B., deJong W.W., and Bloemendal H. Structure and modifications of the junior chaperone α-crystallin. from lens transparency to molecular pathology. Eur. J. Biochem. 225 (1994) 1-19
25. 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
26. Feil I.K., Malfois M., Hendle J., van Der Zandt H., and Svergun D.I. A novel quaternary structure of the dimeric α-crystallin domain with chaperone-like activity. J. Biol. Chem. 276 (2001) 12024-12029
27. Bindels J., Siezen R., and Hoenders H. A model for the architecture of α-crystallin. Ophthalmic Res. 11 (1979) 441-452
28. Tardieu A., Laporte D., Licinio P., Krop B., and Delaye M. Calf lens α-crystallin quaternary structure. a three-layer tetrahedral model. J. Mol. Biol. 192 (1986) 711-724
29. Walsh M., Sen A.C., and Chakrabarti B. Micellar subunit assembly in three layer model of oligomeric α-crystallin. J. Biol. Chem. 266 (1991) 20079-20084
30. Augusteyn R.C., and Koretz J.F. A possible structure for α-crystallin. FEBS Lett. 222 (1987) 1-5
31. Wistow G. Possible tetramer-based quaternary structures for the α-crystallins and small heat shock proteins. Exp. Eye Res. 56 (1993) 729-732
32. InsightII (2000), Accelrys Inc., San Diego, CA
33. van Montfort R., Basha E., Friedrich K.L., Slingsby C., and Vierling E. Crystal structure and assembly of a eukaryotic small heat shock protein. Nat. Struct. Biol. 8 (2001) 1025-1030
34. Feigin L.A., and Svergun D.I. Structure analysis by Small-Angle X-ray, Neutron Scattering (1987), Plenum Press, New York
35. Guinier A., and Fournet G. Small Angle Scattering of X-ray (1955), Wiley, New York
36. Svergun D., and Stuhrmann H. New developments in direct shape determination from small-angle scattering: I. Theory and model calculations. Acta Crystallogr. A47 (1998) 736-744
37. Spinozzi F., Carsughi F., and Mariani P. Particle shape reconstruction by small-angle scattering. Integration of group theory and maximum entropy to multipole expansion method. J. Chem. Phys. 109 (1998) 10148-10158
38. Srinivas V., Raman B., Rao K., Ramakhrisna T., and Rao M. Structural perturbation and enhancement of the chapoerone-like activity of α-crystallin by arginine hydrochloride. Protein Sci. 12 (2003) 1262-1270
39. Doss-Pepe E., Carew E., and Koretz J. Studies of the denaturation patterns of bovine α-crystallin using an ionic denaturant, guanidine hydrochloride and a non-ionic denaturant, urea. Exp. Eye Res. 67 6 (1998) 657-679
40. Maida V., Bennardini F., Bonomi F., Ganadu M., Iametti S., and Mura G. Dissociation of human αB-crystallin aggregates by thiocyanate is structurally and functionally reversible. J. Protein Chem. 19 4 (2000) 311-318
41. Burgio M., Bennet P., and Koretz J. Heat-induced quaternary transitions in hetero- and homo-polymers of α-crystallin. Mol. Vis. 7 (2001) 228-233
42. Raman B., and Rao C. Chaperone-like activity and temperature-induced structural changes of α-crystallin. J. Biol. Chem. 272 (1997) 23559-23564
43. Cinelli S., Spinozzi F., Itri R., Carsughi F., Onori G., and Mariani P. Structural characterisation of the pH-denatured states of ferricytochromec by synchrotron small angle X-ray scattering. Biophys. J. 81 (2001) 3522-3533
44. Jacrot B., and Zaccai G. Determination of molecular weight by neutron scattering. Biopolymers 20 (1976) 2413-2426
45. 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. 292 2 (2000) 261-272
46. Aquilina J., Benesch J., Bateman O., Slingsby C., and Robinson C. Polidispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in αB-crystallin. Proc. Natl. Acad. Sci. 100 19 (2003) 10611-10616
47. Abgar S., Vanhoudt J., Aerts T., and Clauwaert J. Study of the chaperoning mechanism of bovine lens α-crystallin, a member of the α-Small Heat Shock superfamily. Biophys. J. 80 (2001) 1986-1995