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Molecular chaperones, stress proteins and redox homeostasis
Author(s) -
Papp Eszter,
Nardai Gábor,
Söti Csaba,
Csermely Péter
Publication year - 2003
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520170124
Subject(s) - chaperone (clinical) , heat shock protein , microbiology and biotechnology , protein folding , endoplasmic reticulum , oxidative stress , redox , cytoplasm , protein aggregation , hsp70 , proteostasis , biology , unfolded protein response , periplasmic space , biochemistry , chemistry , medicine , organic chemistry , pathology , gene , escherichia coli
Protection against oxidative stress is highly interrelated with the function of the most ancient cellular defense system, the network of molecular chaperones, heat shock, or stress‐proteins. These ubiquitous, conserved proteins help other proteins and macromolecules to fold or re‐fold and reach their final, native conformation. Redox regulation of protein folding becomes especially important during the preparation of extracellular proteins to the outside oxidative milieu, which should take place in a gradual and step‐by‐step controlled manner in the endoplasmic reticulum or in the periplasm. Several chaperones, such as members of the Hsp33 family in yeast and the plethora of small heat shock proteins as well as one of the major chaperones, Hsp70 are able to act against cytoplasmic oxidative damage. Abrupt changes of cellular redox status lead to chaperone induction. The function of several chaperones is tightly regulated by the surrounding redox conditions. Moreover, our recent data suggest that chaperones may act as a central switchboard for the transmission of redox changes in the life of the cell.