On the nature of the optimal form of the holdase-type chaperone stress response

FEBS Letters

article

Damien Hall¹ 

[1] Laboratory of Biochemistry and Genetics;Institute for Protein Research, Osaka University

关键词: biophysical modelling;    holdase;    molecular chaperones;    protein folding;    small heat shock proteins;   

DOI  :  10.1002/1873-3468.13580

来源: John Wiley & Sons Ltd.

【 摘 要 】

The holdase paradigm of chaperone action involves preferential binding by the chaperone to the unfolded protein state, thereby preventing it from either, associating with other unstable proteins (to form large dysfunctional aggregates), or being degraded by the proteolytic machinery of the cell/organism. In this paper, we examine the necessary physical constraints imposed upon the holdase chaperone response in a cell-like environment and use these limitations to comment on the likely nature of the optimal form of chaperone response in vivo.

【 授权许可】

Unknown