Probing α-crystallin structure using chemical cross-linkers and mass spectrometry

Molecular Vision

Volumn 10, Issue , 2004, Pages 857-866

  Peterson, James J ^a   Young, Malin M ^b   Takemoto, Larry J ^a  

^a KANSAS STATE UNIVERSITY   (United States)

^b SANDIA NATIONAL LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3,3' DITHIOBIS(SUCCINIMIDYL PROPIONATE); ALPHA CRYSTALLIN; CHAPERONE; FORMALDEHYDE; 3,3' DITHIOBIS(SULFOSUCCINIMIDYL PROPIONATE); 3,3'-DITHIOBIS(SULFOSUCCINIMIDYL PROPIONATE); CROSS LINKING REAGENT; PEPTIDE FRAGMENT; SUCCINIMIDE DERIVATIVE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CORRELATION ANALYSIS; COW; CROSS LINKING; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MICELLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; ANIMAL; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; ISOLATION AND PURIFICATION; LENS; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRENATAL DEVELOPMENT; PROTEIN QUATERNARY STRUCTURE;

ALPHA-CRYSTALLINS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROSS-LINKING REAGENTS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FORMALDEHYDE; LENS, CRYSTALLINE; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, QUATERNARY; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUCCINIMIDES;

EID: 16644389981     PISSN: 10900535     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (43)

1. Horwitz J. Alpha-crystallin. Exp Eye Res 2003; 76:145-53.
2. Vanhoudt J, Abgar S, Aerts T, Clauwaert J. Native quaternary structure of bovine alpha-crystallin. Biochemistry 2000; 39:4483-92.
3. Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature 1998; 394:595-9.
4. 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; 8:1025-30.
5. Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci U S A 1992; 89:10449-53.
6. 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; 158:319-25.
7. Head MW, Hurwitz L, Goldman JE. Transcription regulation of alpha B-crystallin in astrocytes: analysis of HSF and AP1 activation by different types of physiological stress. J Cell Sci 1996; 109 (Pt 5):1029-39.
8. Lowe J, McDermott H, Pike I, Spendlove I, Landon M, Mayer RJ. alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease. J Pathol 1992; 166:61-8.
9. Meehan S, Berry Y, Luisi B, Dobson CM, Carver JA, MacPhee CE. Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation. J Biol Chem 2004; 279:3413-9.
10. Goldstein LE, Muffat JA, Cherny RA, Moir RD, Ericsson MH, Huang X, Mavros C, Coccia JA, Faget KY, Fitch KA, Masters CL, Tanzi RE, Chylack LT Jr, Bush AI. Cytosolic beta-amyloid deposition and supranuclear cataracts in lenses from people with Alzheimer's disease. Lancet 2003; 361:1258-65.
11. Tardieu A, Laporte D, Licinio P, Krop B, Delaye M. Calf lens alpha-crystallin quaternary structure. A three-layer tetrahedral model. J Mol Biol 1986; 192:711-24.
12. Augusteyn RC, Koretz JF. A possible structure for alpha-crystallin. FEBS Lett 1987; 222:1-5.
13. Wistow G. Possible tetramer-based quaternary structure for alpha-crystallins and small heat shock proteins. Exp Eye Res 1993; 56:729-32.
14. Carver JA, Aquilina JA, Truscott RJ. A possible chaperone-like quaternary structure for alpha-crystallin. Exp Eye Res 1994; 59:231-4.
15. Farnsworth PN, Frauwirth H, Groth-Vasselli B, Singh K. Refinement of 3D structure of bovine lens alpha A-crystallin. Int J Biol Macromol 1998; 22:175-85.
16. Smulders RH, van Boekel MA, de Jong WW. Mutations and modifications support a 'pitted-flexiball' model for alpha-crystallin. Int J Biol Macromol 1998; 22:187-96.
17. Abgar S, Vanhoudt J, Aerts T, Clauwaert J. Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamily. Biophys J 2001; 80:1986-95.
18. Haley DA, Bova MP, Huang QL, Mchaourab HS, Stewart PL. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J Mol Biol 2000; 298:261-72.
19. Berengian AR, Bova MP, Mchaourab HS. Structure and function of the conserved domain in alphaA-crystallin. Site-directed spin labeling identifies a beta-strand located near a subunit interface. Biochemistry 1997; 36:9951-7.
20. Mchaourab HS, Berengian AR, Koteiche HA. Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the alpha-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface. Biochemistry 1997; 36:14627-34.
21. Berengian AR, Parfenova M, Mchaourab HS. Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3. J Biol Chem 1999; 274:6305-14.
22. Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci U S A 1982; 79:2360-4.
23. Young MM, Tang N, Hempel JC, Oshiro CM, Taylor EW, Kuntz ID, Gibson BW, Dollinger G. High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc Natl Acad Sci U S A 2000; 97:5802-6.
24. Rappsilber J, Siniossoglou S, Hurt EC, Mann M. A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry. Anal Chem 2000; 72:267-75.
25. Bennett KL, Kussmann M, Bjork P, Godzwon M, Mikkelsen M, Sorensen P, Roepstorff P. Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping--a novel approach to assess intermolecular protein contacts. Protein Sci 2000; 9:1503-18.
26. Schilling B, Row RH, Gibson BW, Guo X, Young MM. MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides. J Am Soc Mass Spectrom 2003; 14:834-50.
27. McFall-Ngai MJ, Ding LL, Takemoto LJ, Horwitz J. Spatial and temporal mapping of the age-related changes in human lens crystallins. Exp Eye Res 1985; 41:745-58.
28. Boyle D, Gopalakrishnan S, Takemoto L. Localization of the chaperone binding site. Biochem Biophys Res Commun 1993; 192:1147-54.
29. Koretz JF, Augusteyn RC. Electron microscopy of native and reconstituted alpha crystallin aggregates. Curr Eye Res 1988; 7:25-30.
30. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-54.
31. Delcour J, Papaconstantinou J. A change in alpha-crystallin subunit composition in relation to cellular differentiation in adult bovine lens. Biochem Biophys Res Commun 1970; 41:401-6.
32. Metz B, Kersten GF, Hoogerhout P, Brugghe HF, Timmermans HA, de Jong A, Meiring H, ten Hove J, Hennink WE, Crommelin DJ, Jiskoot W. Identification of formaldehyde-induced modifications in proteins: reactions with model peptides. J Biol Chem 2004; 279:6235-43.
33. Groenen PJ, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur J Biochem 1994; 225:1-19.
34. Augusteyn RC, Putilina T, Seifert R. Quenching of tryptophan fluorescence in bovine lens proteins by acrylamide and iodide. Curr Eye Res 1988; 7:237-45.
35. Hendriks W, Weetink H, Voorter CE, Sanders J, Bloemendal H, de Jong WW. The alternative splicing product alpha Ains-crystallin is structurally equivalent to alpha A and alpha B subunits in the rat alpha-crystallin aggregate. Biochim Biophys Acta 1990; 1037:58-65.
36. Siezen RJ, Bindels JG, Hoenders HJ. The quaternary structure of bovine alpha-crystallin. Chemical crosslinking with bifunctional imido esters. Eur J Biochem 1980; 107:243-9.
37. Kamei A, Hamaguchi T, Matsuura N, Masuda K. Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation. Biol Pharm Bull 2001; 24:96-9.
38. Liang JN, Li XY. Interaction and aggregation of lens crystallins. Exp Eye Res 1991; 53:61-6.
39. Groth-Vasselli B, Kumosinski TF, Farnsworth PN. Computer-generated model of the quaternary structure of alpha crystallin in the lens. Exp Eye Res 1995; 61:249-53.
40. Farnsworth PN, Singh K. Self-complementary motifs (SCM) in alpha-crystallin small heat shock proteins. FEBS Lett 2000; 482:175-9.
41. Ghosh JG, Clark JI. Identification of Functional Domains in the sHSP, Human B Crystallin, Using Protein Pin Arrays and Homology Modeling. ARVO Annual Meeting; 2003 May 4-9; Fort Lauderdale (FL).
42. Sheinerman FB, Norel R, Honig B. Electrostatic aspects of protein-protein interactions. Curr Opin Struct Biol 2000; 10:153-9.
43. Lo Conte L, Chothia C, Janin J. The atomic structure of protein-protein recognition sites. J Mol Biol 1999; 285:2177-98.