Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein.
The C-terminal domain and tail, which is the most conserved region of the alpha-crystallin/small heat shock protein (HSP) family, was obtained from rat alpha A-crystallin, bovine alpha B-crystallin and mouse HSP25. All three domains have primarily beta-sheet conformation and less than 10% of alpha-helix, like the proteins from which they are derived. Whereas the C-terminal part of alpha A-crystallin forms dimers or tetramers, the corresponding regions of alpha B-crystallin and HSP25 form larger aggregates. The heat-protective activity, recently described for the alpha-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.
Merck
K B
KB
Department of Biochemistry, University of Nijmegen, The Netherlands.
Horwitz
J
J
Kersten
M
M
Overkamp
P
P
Gaestel
M
M
Bloemendal
H
H
de Jong
W W
WW
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D003459:Crystallins / Q000737:chemistry / Q000235:genetics*; D004274:DNA, Recombinant / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D003459:Crystallins; D004274:DNA, Recombinant; D006360:Heat-Shock Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins