C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin

Molecular and Cellular Biochemistry

Volumn 308, Issue 1-2, 2008, Pages 85-91

  Kallur, Latha S ^a   Aziz, Atya ^a   Abraham, Edathara C ^a  

^a UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

A crystallin; B crystallin; C Terminal truncation; Heat shock proteins; Molecular chaperones; Subunit exchange

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; PROTEIN SUBUNIT;

ARTICLE; CARBOXY TERMINAL SEQUENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; LENS; MOLECULAR WEIGHT; OLIGOMERIZATION; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

ALPHA-CRYSTALLIN A CHAIN; ALPHA-CRYSTALLIN B CHAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; KINETICS; MOLECULAR WEIGHT; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; TIME FACTORS;

EID: 38649094555     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-007-9615-2     Document Type: Article

References (31)

1. Van der Ouderaa FJ, De Jong WW, Bloemendal H (1973) The amino-acid sequence of the alphaA2 chain of bovine alpha-crystallin. Eur J Biochem 39:207-222
2. Van Der Ouderaa FJ, De Jong WW, Hilderink A, Bloemendal H (1974) The amino-acids sequence of the alphaB2 chain of bovine alpha-crystallin. Eur J Biochem 49:157-168
3. De Jong WW, Terwindt EC, Bloemendal H (1975) The amino acid sequence of the A chain of human alpha-crystallin. FEBS Lett 58:310-313
4. Dubin RA, Ally AH, Chung S, Piatigorsky J (1990) Human alpha B-crystallin gene and preferential promoter function in lens. Genomics 7:594-601
5. Horwitz J (1992) α-Crystallin can function as a molecular chaperone. Proc Natl Acad Sci U S A 89:10449-10453
6. Jakob U, Gaestel M, Engel K, Buchner J (1993) Small heat shock proteins are molecular chaperones. J Biol Chem 268:1517-1520
7. Wang K, Spector A (1994) The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states. J Biol Chem 269:13601-13608
8. Andley UP, Mathur S, Griest TA, Petrash JM (1996) Cloning, expression, and chaperone-like activity of human αA-crystallin. J Biol Chem 271:31973-31980
9. Rao PV, Huang QL, Horwitz J, Zigler JS (1995) Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta 1245:439-447
10. Augusteyn RC (1998) Polymers and polymerization: The view from down under. Int J Biol Macromol 22:253-262
11. Carver JA, Aquilina JA, Truscott RJ, Ralston GB (1992) Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin. FEBS Lett 311:143-149
12. Lindner RA, Treweek TM, Carver JA (2001) The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin. Biochem J 354:79-87
13. Kramps JA, De Jong WW, Wollensak J, Hoenders HJ (1978) The polypeptide chains of alpha-crystallin from old human eye lenses. Biochim Biophys Acta 533:487-495
14. Takemoto L, Emmons T (1991) Truncation of αA-crystallin from the human lens. Exp Eye Res 53:811-813
15. Groenen PJ, Merck KB, De Jong WW, Bloemendal H (1994) Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology. Eur J Biochem 225:1-19
16. Takemoto LJ (1995) Identification of the in vivo truncation sites at the C-terminal region of alpha-A crystallin from aged bovine and human lens. Curr Eye Res 14:837-841
17. Lund AL, Smith JB, Smith DL (1996) Modifications of the water-insoluble human lens alpha-crystallins. Exp Eye Res 63:661-672
18. Colvis C. Garland D (2002) Posttranslational modification of human αA-crystallin: Correlation with electrophoretic migration. Arch Biochem Biophys 397:319-323
19. Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, Smith JB (1998) Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 67:21-30
20. Miesbauer LR, Zhou X, Yang Z, Yang Z, Sun Y, Smith DL, Smith JB (1994) Post-translational modifications of water-soluble human lens crystallins from young adults. J Biol Chem 269:12494-12502
21. Takemoto LJ (1998) Quantitation of specific cleavage sites at the C-terminal region of alpha-A crystallin from human lenses of different age. Exp Eye Res 66(1998):263-266
22. Thampi P, Hassan A, Smith JB, Abraham EC (2002) Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. Invest Ophthalmol Vis Sci 43:3265-3272
23. Shroff NP, Bera S, Cherian-Shaw M, Abraham EC (2001) Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of alphaB-crystallin. Mol Cell Biochem 220:127-133
24. Shroff NP, M. Cherian M, Abraham EC (1998) The role of methionine residues in the oxidation-mediated decrease in chaperone activity. Invest Ophthalmol Visual Sci 39:S1018
25. Shroff NP (1999) Ph.D. Thesis, Medical College of Georgia, Augusta, GA
26. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
27. Bera S, Abraham EC (2002) The alphaA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with alphaB-crystallin. Biochemistry 41:297-305
28. Shroff NP, Cherian-Shaw M, Bera S, Abraham EC (2000) Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function. Biochemistry 39:1420-1426
29. Kelley PB, Abraham EC (2003) Thermally induced disintegration of the oligomeric structure of alphaB-crystallin mutant F28S is associated with diminished chaperone activity. Mol Cell Biochem 252:273-278
30. Brady JP, Garland D, Y. Duglas-Tabor Y, Groome A, Wawrousek EF (1997) Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin. Proc Natl Acad Sci U S A 94:884-889
31. Aziz A, Santhoshkumar P, Sharma K K, Abraham EC (2007) Cleavage of the C-terminal serine of human αA-crystallin produces αA 1-172 with increased chaperone activity and oligomeric size. Biochemistry 46:2510-2519