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
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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