The small heat-shock protein, αB-Crystallin, has a variable quaternary structure

Journal of Molecular Biology

Volumn 277, Issue 1, 1998, Pages 27-35

  Haley, Dana A ^a   Horwitz, Joseph ^a   Stewart, Phoebe L ^a  

^a Dept Molec Med Pharmacol C ^*  (United States)

Author keywords

Alpha B crystallin; Cryo electron microscopy; Image classification; Small heat shock protein; Three dimensional reconstruction

Indexed keywords

ALPHA BETA CRYSTALLIN; CRYSTALLIN; HEAT SHOCK PROTEIN; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; GEL FILTRATION CHROMATOGRAPHY; LENS; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

EID: 0032549677     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1611     Document Type: Article

References (53)

1. Adrian M., Dubochet J., Lepault J., McDowall A.W. Cryo-electron microscopy of viruses. Nature. 308:1984;32-36
2. Augusteyn R.C., Koretz J.F. A possible structure for α-crystallin. FEBS Letters. 222:1987;1-5
3. Bax B., Lapatto R., Nalini V., Driessen H., Lindley P.F., Mahadevan D., Blundell T.L., Slingsby C. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature. 347:1990;776-780
4. Behlke J., Lutsch G., Gaestel M., Bielka H. Supramolecular structure of the recombinant murine small heat shock protein hsp25. FEBS Letters. 288:1991;119-122
5. Berengian A.R., Bova M.P., Mchaourab H.S. Structure and function of the conserved domain in αA-crystallin. Site-directed spin labeling identifies a β-strand located near a subunit interface. Biochemistry. 36:1997;9951-9957
6. Bindels J.G., Siezen R.J., Hoenders H.J. A model for the architecture of α-crystallin. Ophthal. Res. 11:1979;441-452
7. Bloemendal H., Zweers A., Benedetti E.L., Walters H. Selective reassociation of the crystallins. Expt. Eye Res. 20:1975;463-478
8. Blundell T., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., Turnell B., Wistow G. The molecular structure and stability of the eye lens X-ray analysis of the γ-crystallin II. Nature. 289:1981;771-777
9. Böttcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 386:1997;88-91
10. Bova M.P., Ding L.L., Horwitz J., Fung B.K.-K. Subunit exchange of αA-crystallin. J. Biol. Chem. 272:1997;29511-29517
11. 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens α-crystallin. FEBS Letters. 311:1992;143-149
12. Carver J.A., Aquilina J.A., Truscott R.J.W. A possible chaperone-like quaternary structure for α-crystallin. Expt. Eye Res. 59:1994;231-234
13. 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. FEBS Letters. 369:1995;305-310
14. Caspers G.-J., Leunissen J.A.M., de Jong W.W. The expanding small heat-shock protein family, and structure predictions of the conserved "α-crystallin domain" J. Mol. Evol. 40:1995;238-248
15. Chiesi M., Longoni S., Limbruno U. Cardiac alpha-crystallin. III. Involvement during heart ischemia. Mol. Cell. Biochem. 97:1990;129-136
16. Conway J.F., Cheng N., Zlotnick A., Wingfield P.T., Stahl S.J., Steven A.C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 386:1997;91-94
17. de Jong W.W., Lubsen N.H., Kraft H.J. Molecular evolution of the eye lens. Prog. Retinal Eye Res. 13:1994;391-442
18. Deretic D., Aebersold R.H., Morrison H.D., Papermaster D.S. αA- and αB-crystallin in the retina. Association with the post-golgi compartment of frog retinal photoreceptors. J. Biol. Chem. 269:1994;16853-16861
19. Groenen P.J.T.A., Merck K.B., de Jong W.W., Bloemendal H. Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology. Eur. J. Biochem. 225:1994;1-19
20. Groth-Vasselli B., Kumosinski T.F., Farnsworth P.N. Computer-generated model of the quaternary structure of alpha crystallin in the lens. Expt. Eye Res. 61:1995;249-253
21. Harauz G., van Heel M. Exact filters for general geometry three dimensional reconstruction. Optik. 73:1986;146-156
22. Head M.W., Corbin E., Goldman J.E. Coordinate and independent regulation of αB-crystallin and Hsp27 expression in response to physiological stress. J. Cell. Physiol. 159:1994;41-50
23. Horwitz J. α-Crystallin can function as a molecular chaperone. Proc. Natl Acad. Sci. USA. 89:1992;10449-10453
24. Horwitz J., Huang Q.-L., Ding L., Bova M.P. Lens alpha-crystallin chaperone-like properties. Methods Enzymol. 1998;. In the press
25. Ingolia T.D., Craig E.A. Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl Acad. Sci. USA. 79:1982;2360-2364
26. Jakob U., Gaestel M., Engel K., Buchner J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268:1993;1517-1520
27. Koretz J.F., Augusteyn R.C. Electron microscopy of native and reconstituted alpha crystallin aggregates. Curr. Eye Res. 7:1988;25-30
28. Lamba O.P., Borchman D., Sinha S.K., Shah J., Renugopalakrishnan V., Yappert M.C. Estimation of the secondary structure and conformation of bovine lens crystallins by infrared spectroscopy quantitative analysis and resolution by Fourier self-deconvolution and curve fit. Biochim. Biophys. Acta. 1163:1993;113-123
29. Lata K.R., Agrawal R.K., Penczek P., Grassucci R., Zhu J., Frank J. Three-dimensional reconstruction of the Escherichia coli 30 S ribosomal subunit in ice. J. Mol. Biol. 262:1996;43-52
30. Longoni S., Lattonen S., Bullock G., Chiesi M. Cardiac alpha-crystallin. II. Intracellular localization. Mol. Cell. Biochem. 97:1990;121-128
31. Mancini E.J., de Haas F., Fuller S.D. High-resolution icosahedral reconstruction fulfilling the promise of cryo-electron microscopy. Structure. 5:1997;741-750
32. Merck K.B., de Haard-Hoekman W.A., Oude Essink B.B., Bloemendal H., de Jong W.W. Expression and aggregation of recombinant αA-crystallin and its two domains. Biochim. Biophys. Acta. 1130:1992;267-276
33. Merck K.B., Groenen P.J.T.A., Voorter C.E.M., de Haard-Hoekman W.A., Horwitz J., Bloemendal H., de Jong W.W. Structural and functional similarities of bovine α-crystallin and mouse small heat-shock protein. J. Biol. Chem. 268:1993;1046-1052
34. Phillips M.L., Pullinger C., Kroes I., Kroes J., Hardman D.A., Chen G., Curtiss L.K., Gutierrez M.M., Kane J.P., Schumaker V.N. A single copy of apolipoprotein B-48 is present on the human chylomicron remnant. J. Lipid Res. 38:1997;1170-1177
35. Rao P.V., Huang Q., Horwitz J., Zigler J.S. Jr. Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim. Biophys. Acta. 1245:1995;439-447
36. Renkawek K., Voorter C.E.M., Bosman G.J.C.G., van Workum F.P.A., de Jong W.W. Expression of αB-crystallin in Alzheimer's disease. Acta Neuropathol. 87:1994;155-160
37. Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251
38. Siezen R.J., Argos P. Structural homology of lens crystallins. III. Secondary structure estimation from circular dichroism and prediction from amino acid sequences. Biochim. Biophys. Acta. 748:1983;56-67
39. Siezen R.J., Hoenders H.J. The quaternary structure of bovine α-crystallin. Surface probing by limited proteolysis in vitro. Eur. J. Biochem. 96:1979;431-440
40. Srinivasan A.N., Nagineni C.N., Bhat S.P. αA-crystallin is expressed in non-ocular tissues. J. Biol. Chem. 267:1992;23337-23341
41. Stark H., Rodnina M.V., Rinke-Appel J., Brimacombe R., Wintermeyer W., van Heel M. Visualization of elongation factor Tu on the Escherichia coli ribosome. Nature. 389:1997;403-406
42. Stewart P.L., Fuller S.D., Burnett R.M. Difference imaging of adenovirus bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J. 12:1993;2589-2599
43. Stewart P.L., Chiu C.Y., Huang S., Muir T., Zhao Y., Chait B., Mathias P., Nemerow G.R. Cryo-EM visualization of an exposed RGD epitope on adenovirus that escapes antibody neutralization. EMBO J. 16:1997;1189-1198
44. Tardieu A., Laporte D., Licinio P., Krop B., Delaye M. Calf lens α-crystallin quaternary structure. A three-layer tetrahedral model. J. Mol. Biol. 192:1986;711-724
45. van den Oetelaar P.J.M., van Someren P.F.H.M., Thomson J.A., Siezen R.J., Hoenders H.J. A dynamic quaternary structure of bovine α-crystallin as indicated from intermolecular exchange of subunits. Biochemistry. 29:1990;3488-3493
46. van Heel M., Harauz G., Orlova E.V., Schmidt R., Schatz M. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116:1996;17-24
47. van Noort J.M., van Sechel A.C., Bajramovic J.J., Ouagmiri M.E., Polman C.H., Lassmann H., Ravid R. The small heat-shock protein αB-crystallin as candidate autoantigen in multiple sclerosis. Nature. 375:1995;798-801
48. Vérétout F., Delaye M., Tardieu A. Molecular basis of eye lens transparency. J. Mol. Biol. 205:1989;713-728
49. Walsh M.T., Sen A.C., Chakrabarti B. Micellar subunit assembly in a three-layer model of oligomeric α-crystallin. J. Biol. Chem. 266:1991;20079-20084
50. Wang K., Spector A. The chaperone activity of bovine α crystallin. J. Biol. Chem. 269:1994;13601-13608
51. Wistow G. Possible tetramer-based quaternary structures for the α-crystallins and small heat shock proteins. Expt. Eye Res. 56:1993;729-732
52. Xia J.Z., Aerts T., Doncell K., Clauwaert J. Light scattering by bovine α-crystallin proteins in solutions hydrodynamic structure and interparticle interaction. Biophys. J. 66:1994;861-872
53. Yoshida H., Yumoto N., Tsukahara I., Murachi T. The degradation of α-crystallin at its carboxyl-terminal portion by calpain in bovine lens. Invest. Ophthalmol. Vis. Sci. 27:1986;1269-1273