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On the nature of the optimal form of the holdase‐type chaperone stress response
Author(s) -
Hall Damien
Publication year - 2020
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 - 10.1002/1873-3468.13580
Subject(s) - chaperone (clinical) , microbiology and biotechnology , protein folding , dysfunctional family , biophysics , chemistry , biology , medicine , clinical psychology , pathology
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 .