Dissociation is not required for α-crystallin's chaperone function

Experimental Eye Research

Volumn 79, Issue 6, 2004, Pages 781-784

  Augusteyn, R C ^a,b  

^a LA TROBE UNIVERSITY   (Australia)

^b UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

Crystallin; chaperone; crosslinking; dissociation

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; GLUTARALDEHYDE;

CHROMATOGRAPHY; CONFERENCE PAPER; CONTROLLED STUDY; CROSS LINKING; DISSOCIATION; MOLECULAR INTERACTION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRECIPITATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION;

ALPHA-CRYSTALLINS; ANIMALS; CATTLE; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN DENATURATION;

EID: 11844277108     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2004.08.010     Document Type: Conference Paper

References (20)

1. R.C. Augusteyn, T.P. Hum, T. Putilin, and J.A. Thomson The location of sulphydryl groups in α-crystallin Biochim. Biophys. Acta 915 1987 132 139
2. R.C. Augusteyn, E. Parkhill, and A. Stevens The effects of isolation conditions on the properties of α-crystallin Exp. Eye Res. 54 1992 219 228
3. R.C. Augusteyn, K.P. Ghiggino, and T.P. Putilina Studies on the location of aromatic amino acids in α-crystallin Biochim. Biophys. Acta 1162 1993 61 71
4. M. Cherian, and E.C. Abraham Decreased molecular chaperone property of α-crystallin due to posttranslational modification Biochem. Biophys. Res. Commun. 208 1995 675 679
5. K.P. Das, and W.K. Surewicz Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin FEBS Lett. 369 1995 321 325
6. J. Horwitz Alpha-crystallin can function as a molecular chaperone Proc. Natl Acad. Sci. USA 89 1992 10449 10453
7. M.J. Kelley, L.L. David, N. Iwasaki, J. Wright, and T.R. Shearer α-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract J. Biol. Chem. 268 1993 18844 18849
8. K.K. Kim, R. Kim, and S.H. Kim Crystal structure of a small heat-shock protein Nature 394 1998 595 599
9. R. Klemenz, E. Frhli, R.H. Steiger, R. Schafer, and A. Aovama Alpha B-crystallin is a small heatshock protein Proc. Natl Acad. Sci. USA 88 1991 3652 3656
10. R.S. Kumar, and K.K. Sharma Synthetic αA-crystallin's functional element has chaperone-like activity toward oxidized γ-crystallin J. Pept. Res. 56 2000 157 164
11. 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
12. K.B. Merck, P.J. Groenen, C.E. Voorter, W.A. de Haard-Hoekman, J. Horwitz, H. Bloemendal, and W.W. de Jong Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones J. Biol. Chem. 268 1993 1046 1052
13. M.L. Plater, D. Goode, and M.J. Crabbe Effects of site-directed mutations on the chaperone-like activity of αB-crystallin J. Biol. Chem. 271 1996 28558 28566
14. B. Raman, and C.M. Rao Chaperone-like activity and quaternary structure of alpha-crystallin J. Biol. Chem. 269 1994 27264 27268
15. J.A. Schaurte, and A. Gafni Photodegradation of tryptophan residues and attenuation of molecular chaperone activity in alpha-crystallin are correlated Biochem. Biophys. Res. Commun. 212 1995 900 905
16. K.K. Sharma, and B.J. Ortwerth Effect of crosslinking on the chaperone-like function of alpha crystallin Exp. Eye Res. 61 1995 413 421
17. K.K. Sharma, G.S. Kumar, A.S. Murphy, and K. Kester Identification of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in alpha-crystallin J. Biol. Chem. 273 1998 15474 15478
18. K.K. Sharma, R.S. Kumar, G.S. Kumar, and P.T. Quinn Synthesis and characterization of a peptide Identified as a functional element in αA-crystallin J. Biol. Chem. 275 2000 3767 3771
19. m- crystallin: the reversibility of urea-dissociation J. Biol. Chem. 259 1984 4339 4345
20. R.L.M. van Montford, E. Basha, K.L. Friedrich, C. Slingsby, and E. Vierling Crystal structure and assembly of a eukaryotic small heat shock protein Nature. Struct. Biol. 8 2002 1025 1030