Characteristics of super αA‐crystallin, a product of in vitro exon shuffling

FEBS Letters

Boelens, Wilbert C.¹  Bloemendal, Hans¹  de Jong, Wilfried W.¹  Renkema, Wouter¹  van Rijk, Anke F.¹  van den Hurk, Maarten J.J.¹ 

[1] Department of Biochemistry, University of Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands

关键词: Mutant αA-crystallin;    Small heat shock protein;    Exon shuffling;   

DOI  :  10.1016/S0014-5793(00)01908-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown