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Characteristics of super αA‐crystallin, a product of in vitro exon shuffling
Author(s) -
van Rijk Anke F.,
van den Hurk Maarten J.J.,
Renkema Wouter,
Boelens Wilbert C.,
de Jong Wilfried W.,
Bloemendal Hans
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01908-6
Subject(s) - chaperone (clinical) , thermostability , crystallin , chemistry , hsp70 , exon , mutant , protein subunit , biochemistry , heat shock protein , microbiology and biotechnology , biophysics , biology , gene , medicine , pathology , enzyme
αA‐Crystallin, a small heat shock protein with chaperone‐like activity, forms dynamic multimeric complexes. Recently we described the spontaneous generation of a mutant protein (super αA‐crystallin) by exon duplication arisen via exon shuffling confirming a classic hypothesis by Gilbert [Nature 271 (1978) 501]. Comparison of super αA‐crystallin, which is viable in a mouse skeletal muscle cell line, with normal αA‐crystallin shows that it has diminished thermostability, increased exposure of hydrophobic patches, a larger complex size and lost its chaperone activity. However, super αA‐crystallin subunits exchange as readily between complexes as does normal αA‐crystallin. These data indicate that chaperone‐like activity may vanish independent of subunit hydrophobicity and exchangeability.