Abstract
The C-terminal domain and tail, which is the most conserved region of the α-crystallin/small heat shock protein (HSP) family, was obtained from rat αA-crystallin, bovine αB-crystallin and mouse HSP25. All three domains have primarily β-sheet conformation and less than 10% of α-helix, like the proteins from which they are derived. Whereas the C-terminal part of αA-crystallin forms dimers or tetramers, the corresponding regions of αB-crystallin and HSP25 form larger aggregates. The heat-protective activity, recently described for the α-crystallin/small HSP family, is not retained in the C-terminal domain and tail. In the course of this study some differences with the previously published sequence of HSP25 were observed, and a revision is proposed.
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Abbreviations
- αA2Dt:
-
residues 64–173 of rat α-crystallin
- αB2Dt:
-
residues 70–175 of bovine αB-crystallin
- bp:
-
base pair
- HSP2Dt:
-
residues 92–209 of HSP25
- HSP(s):
-
heat shock protein(s)
- HSP25:
-
mouse small HSP
- PCR:
-
polymerase chain reaction
- PMSF:
-
phenylmethylsulfonyl chloride
- SDS:
-
sodium dodecyl sulfate; polyacrylamide
- WSF:
-
water-soluble fraction
References
Ingolia TD & Craig EA (1982) Proc. Natl. Acad. Sci. USA 79: 2360–2364
De Jong WW, Leunissen JAM & Voorter CEM (1993) Mol. Biol. Evol. 10: 103–116
Horwitz J (1992) Proc. Natl. Acad. Sci. USA 89: 10449–10453
Merck KB, Groenen PJTA, Voorter CEM, De Haard-Hoekman WA, Horwitz J, Bloemendal H & De Jong WW (1993) J. Biol. Chem. 268: 1046–1052
Jakob U, Gaestel M, Engel K & Buchner J (1993) J. Biol. Chem. 268: 1517–1520
Bindels JG, Siezen RJ & Hoenders HJ (1979) Ophthalmic Res. 11: 441–452
Tardieu A, Laporte D, Licinio P, Krop B & Delaye M (1986) J. Mol. Biol. 192: 711–724
Augusteyn RC & Koretz JF (1987) FEBS Lett. 222: 1–5.
Walsh MT, Sen AC & Chakrabarti B (1991) J. Biol. Chem. 266: 20079–20084
Wistow G (1985) FEBS Lett. 181: 1–6
Merck KB, De Haard-Hoekman WA, Oude Essink BB, Bloemendal H & De Jong WW (1992)Biochim. Biophys. Acta 1130: 267–276
Wistow GJ (1993) Exp. Eye Res. (in press)
Boyer HW & Poulland-Dussoix D (1969) J. Mol. Biol. 41: 459–472
Gibson TJ (1984) Studies on the Epstein-Barr virus genome. Ph.D. Thesis Cambridge University, Cambridge
Gaestel M, Gross B, Benndorf R, Strauss M, Schunk W, Kraft R, Otto A, Bohm H, Stahl J, Drabsch H & Bielka H (1989) Eur. J. Biochem. 179: 209–213
Studier FW, Rosenberg AH, Dunn JJ & Dubendorff JW (1989) Methods Enzymol. 185: 60–89
Sanger F, Nicklen S & Coulson AR (1977) Proc. Natl. Acad. Sci. USA 74: 5463–5467
De Jong WW, Zweers A, Versteeg M & Nuy-Terwindt EC (1984) Eur. J. Biochem. 141: 131–140
Gaestel M, Schröder W, Benndorf R, Lippmann C, Buchner K, Hucho F, Erdmann VA & Bielka H (1991) J. Biol. Chem. 266: 14721–14724
Lavoie J, Chrétien P & Landry J (1990) Nucleic Acids Res. 18: 1637
Hickey E, Brandon SE, Potter R, Stein G, Stein J & Weber LA (1986) Nucleic Acids Res. 14: 4127–4145
Carper SW, Rocheleau TA & Storm FK (1990) Nucleic Acids Res. 18: 6457
Dyson HJ, Merutka G, Waltho JP, Lerner RA & Wright PE (1992) J. Mol. Biol. 226: 795–817
Gething M-J & Sambrook J (1992) Nature 355: 33–45
Carver JA, Aquilina JA, Truscott RJW & Ralston GB (1992) FEBS Lett. 311: 143–149
Gaestel M, Gotthardt R & Müller T (1993) Gene (in press)
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Merck, K.B., Horwitz, J., Kersten, M. et al. Comparison of the homologous carboxy-terminal domain and tail of α-crystallin and small heat shock protein. Mol Biol Rep 18, 209–215 (1993). https://doi.org/10.1007/BF01674432
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DOI: https://doi.org/10.1007/BF01674432