Acetylation of α-crystallin with N-acetylimidazole and its influence upon the native aggregate and subunit reassembly

Current Eye Research

Volumn 19, Issue 4, 1999, Pages 358-367

  Pal, Jaya ^a   Bera, Sibes ^a   Ghosh, Sudhir K ^a  

^a SAHA INSTITUTE OF NUCLEAR PHYSICS   (India)

Author keywords

Acetylation; Molten globule like aggregate; N acetylimidazole; Native aggregate; Subunit reassembly; crystallin

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; LENS PROTEIN; N ACETYLIMIDAZOLE; PROTEIN SUBUNIT; TYROSINE;

ACETYLATION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ELECTROPHORETIC MOBILITY; FLUORESCENCE SPECTROSCOPY; GEL ELECTROPHORESIS; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR SIZE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DENATURATION; PROTEIN FOLDING; ULTRAVIOLET SPECTROSCOPY;

EID: 0032694877     PISSN: 02713683     EISSN: None     Source Type: Journal    
DOI: 10.1076/ceyr.19.4.358.5299     Document Type: Article

References (35)

1. Hoenders HJ, Bloemendal H Aging of the lens proteins. In Bloemendal ed, Molecular and Cellular Biology of the Eye Lens. John Wiley and Sons, New York 1981: 279-339.
2. Harding, J. Cataract: Biochemistry, Epidemiology and Pharmacology. Chapman and Hall, London, 1991: 1-70.
3. Spector A. Aggregation of α-crystallin and its possible relationship to cataract formation. Israel J Med Sci. 1972;8:1577-1582.
4. 2 chain of bovine α-crystallin. Eur J Biochem. 1973;39:207-222.
5. 2 chain of bovine α-crystallin. Eur J Biochem. 1974;49:157-168.
6. Siezen RJ, Bindels JG, Hoender HJ. The quaternary structure of bovine α-crystallin: Size charge microheterogeneity: More than 1000 different hybrids? Eur J Biochem. 1978;91:387-396.
7. Siezen RJ, Berger H. The quaternary structure of bovine α-crystallin: Size and shape studies by sedimentation, small-angle x-ray scattering and quasi-elastic light scattering. Eur J Biochem. 1978;91:397-405.
8. Doss Kathleen AW, Koretz JF. Preliminary studies on the aggregation process of α-crystallin. Exp Eye Res. 1997;65:255-266.
9. Horwitz J. α-Crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992;89:10449-10453.
10. Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc Natl Acad Sci USA. 1982;79:2360-2364.
11. Siezen RJ, Bindels J, Hoenders HJ. (1980) The quaternary structure of bovine α-crystallin: effects of variation in alkaline pH, ionic strength, temperature and calcium concentration. Eur J Biochem. 1980;111:435-444.
12. Tardieu A, Laporte D, Licinio P, Krop B, Delaye M. Calf lens α-crystallin quaternary structure: a three layer tetrahedral model. J Mol Biol. 1986;192:711-724.
13. Augusteyn RC, Koretz JF. A possible structure of α-crystallin. FEBS Lett. 1987;222:1-5.
14. Walsh MT, Sen AC, Chakrabarti B. Micellar subunit assembly in a three layered model oligomeric α-crystallin. J Biol Chem. 1981;266:20079-20084.
15. Haley D.A., Horwitz, J. and Stewart, P.L. The small heat-shock protein, αB-crystallin, has a variable quaternary structure, J. Mol. Biol. 1998;277:27-35.
16. Kim KK, Kim R, Kim S-H. Crystal structure of a small heat shock protein. Nature. 1998;394:595-599.
17. Roy B, Ghosh SK. Purification and properties of the low molecular weight α-crystallin from normal goat lens: comparison with bovine lens. Exp Eye Res. 1991;53:693-701.
18. Bera S, Ghosh SK. Histidine residues in α-crystallin are not all available for chemical modification and acid-base titration. J Protein Chem. 1996;15:585-590.
19. Bjork I. Studies on γ-crystallin from calf lens. I. Isolation by gel filtration. Exp Eye Res. 1961;1:145-154.
20. Bjork I. Studies on γ-crystallin from calf lens. II. Purification and some properties of the main protein components. Exp Eye Res. 1964;3:254-261.
21. Riordan JF, Waeker WEC, Vallee BL. N-acetylimidazole: A reagent for determination of 'free' tyrosyl residues of proteins. Biochemistry. 1965;4:1758-1765.
22. Bera S, Pal J, Roy B, Ghosh SK. Chemical modifications and dissociation characteristics of tyrosine and tryptophan residues in α-crystallin. Ind J Biochem Biophys. 1997;34:419-428.
23. Hestrin S. The reaction of acetylcholine and other carboxylic acid derivatives with hydroxylamine, and its analytical application. J Biol Chem. 1949;180:249-261.
24. Laemmli UK. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
25. Raman B, Ramakrishna T, Rao CM. Temperature dependent chaperone-like activity of α-crystallin. FEBS Lett. 1995;365:133-136.
26. Das KP, Surewicz WK. Temperature induced exposure of hydrophobic surfaces and its effect on chaperone activity of α-crystallin. EFBS Lett. 1995;369:321-325.
27. ins-crystallin in structurally equivalent to αA and αB subunits in the rat α-crystallin aggregate. Biochim Biophys Acta. 1990;1037:58-65
28. Augusteyn RC, Ghiggino KP, Putilina T. Studies on the location of aromatic amino acids in α-crystallin. Biochim Biophys Acta. 1993;1162:61-71.
29. Augusteyn RC, Hum TP, Putilina T, Thomson JA. The location of sulphydryl groups in α-crystallin. Biochim Biophys Acta. 1987;915:132-139.
30. Pal J, Ghosh SK. Influence of chemical modification of cysteine and histidine side chains upon subunit reassembly of α-crystallin J Protein Chem. 1998;17:617-632.
31. Strickland EH. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit Rev Biochem. 1974;2:113-175.
32. Raman B, Ramakrishna T, Rao CM. Chaperone-like activity and temperature-induced structural changes of α-crystallin. J Biol Chem. 1997;272:23559-23564.
33. Das BK, Liang JJ, Chakrabarti B. Heat-induced conformational change and increased chaperone activity of lens α-crystallin. Curr Eye Res. 1997;16:303-309.
34. Thomson JA, Augusteyn RC. On the structure of α-crystallin: the minimum molecular weight. Curr Eye Res. 1988;7:563-569.
35. de Jong WW, Zweers A, Cohen LH. Influence of single amino acid substitution on electrophoretic mobility of sodium dodecyl sulfate-protein complexes, Biochem Biophys Res Commun. 1978;82:532-539.