X-ray- and neutron-scattering studies of α-crystallin and evidence that the target protein sits in the fenestrations of the α-crystallin shell

Investigative Ophthalmology and Visual Science

Volumn 48, Issue 6, 2007, Pages 2695-2700

  Regini, Justyn W ^a   Grossmann, J Günter ^b   Timmins, Peter ^c   Harding, John J ^d   Quantock, Andrew J ^a   Hodson, Stuart A ^d   Elliot, Gerald F ^a,d  

^a CARDIFF UNIVERSITY   (United Kingdom)

^b DARESBURY LABORATORY   (United Kingdom)

^c INSTITUT LAUE LANGEVIN   (France)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; DEUTERIUM;

ARTICLE; FENESTRATION; HYDROGEN BOND; LENS; NEUTRON SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN TARGETING; RADIATION SCATTERING; SPECTROPHOTOMETRY; TEMPERATURE; ANIMAL; CATTLE; CHEMISTRY; METHODOLOGY; NEUTRON DIFFRACTION; PROTEIN BINDING; X RAY DIFFRACTION;

ALPHA-CRYSTALLINS; ANIMALS; BETA-CRYSTALLINS; CATTLE; MOLECULAR CHAPERONES; NEUTRON DIFFRACTION; PROTEIN BINDING; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION;

EID: 34347205682     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.06-0559     Document Type: Article

References (27)

1. de Jong WW. Molecular and Cellular Biology of the Eye Lens. New York; 1981.
2. Bhat SP, Nagineni CN. alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun. 1989;158:319-325.
3. Kato K, Shinohara H, Kurobe N, Inaguma Y, Shimizu Y, Oshima K. Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system. Biochim Biophys Acta. 1991;1074:201-208.
4. Harding J. Cataract: Biochemistry, Epidemiology and Pharmacology. London: Chapman and Hall; 1991.
5. Delaye M, Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature. 1983;302:415-417.
6. Farahbakhsh ZT, Huang QL, Ding LL, et al. Interaction of alpha-crystallin with spin-labeled peptides. Biochemistry. 1995;34:509-516.
7. Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992;89:1449-1453.
8. Heath MM, Rixon KC, Harding JJ. Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin. Biochim Biophys Acta. 1996;1315: 176-184.
9. Chiesi M, Longoni S, Limbrruno U. Cardiac alpha-crystallin. III. Involvement during heart ischemia. Mol Cell Biochem. 1990;97: 129-136.
10. van Noort JM, van Sechel AC, Bajramovic JJ, et al. The small heat-shock protein alpha B-crystallin as candidate autoantigen in multiple sclerosis. Nature. 1995;375:798-801.
11. Regini JW, Grossman JG, Burgio MR, et al. Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction. J Mol Biol. 2004;336:1185-1194.
12. Burgio MR, Kim CJ, Dow CC, Koretz JF. Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature. Biochem Biophys Res Commum. 2000; 268:426-432.
13. Derham BK, Harding JJ. Effects of modifications of alpha-crystallin on its chaperone and other properties. Biochem J. 2002;364:711-717.
14. Guinier A, Fournet F. Small Angle Scattering of X-Rays. New York: Wiley Interscience; 1955.
15. Ganea E, Harding JJ. Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. Eur J Biochem. 1995;231:181-185.
16. Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature. 1998;394:595-599.
17. van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. Crystal structure and assembly of a eukaryotic small heat shock protein. Nat Struct Biol. 2001;8:1025-1030.
18. Chalikian TV, Totrov M, Abagyan R, Breslauer KJ. The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data. J Mol Biol. 1996;260:588-603.
19. Haley DA, Horwitz J, Stewart PL. Image restrained modeling of alphaB-crystallin. Exp Eye Res. 1999;68:133-136.
20. Carver JA, Aquilina JA, Truscott RJ. A possible chaperone-like quaternary structure for alpha-crystallin. Exp Eye Res. 1994;59: 231-234.
21. Spinozzi F, Mariani P, Rustichelli F, et al. Temperature dependence of chaperone-like activity and oligomeric state of alphaB-crystallin. Biochim Biophys Acta. 2006;1764:667-687.
22. Lindner RA, Treweek TM, Carver JA. The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin. Biochem J. 2001;354:79-87.
23. Bova MP, Ding L-L, Horwitz J, Fung, BK-K. Subunit exchange of alphaA-crystallin. J Biol Chem. 1997;272:29511-29517.
24. Liu L, Ghosh JG, Clark JI, Jiang S. Studies of alphaB-crystallin subunit dynamics by surface plasmon resonance. Anal Biochem. 2006;350:186-195.
25. Cioni P, Strambini GB. Effect of heavy water on protein flexibility. Biophys J. 2002;82:3246-3253.
26. Vanhoudt J, Aerts T, Abgar S, Clauwert J. Quaternary structure of bovine alpha-crystallin: influence of temperature. Int J Biol Macromol. 1998;22:229-273.
27. Vanhoudt J, Abgar S, Aerts T, Clauwert J. Native quaternary structure of bovine α-crystallin. Biochemistry. 2000;39:4483-4492.