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Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage.

ABSTRACT: How proteins fold and are protected from stress-induced aggregation is a long-standing mystery and a crucial question in biology. Here, we present the current knowledge on the chaperedoxin CnoX, a novel type of protein folding factor that combines holdase chaperone activity with a redox protective function. Focusing on Escherichia coli CnoX, we explain the essential role played by this protein under HOCl (bleach) stress, discussing how it protects its substrates from both aggregation and irreversible oxidation, which could otherwise interfere with refolding. Finally, we highlight the unique ability of CnoX, apparently conserved during evolution, to cooperate with the GroEL/ES folding machinery.

SUBMITTER: Dupuy E

PROVIDER: S-EPMC8129009 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage.

Dupuy Emile E Collet Jean-François JF

Frontiers in molecular biosciences 20210504

How proteins fold and are protected from stress-induced aggregation is a long-standing mystery and a crucial question in biology. Here, we present the current knowledge on the chaperedoxin CnoX, a novel type of protein folding factor that combines holdase chaperone activity with a redox protective function. Focusing on <i>Escherichia coli</i> CnoX, we explain the essential role played by this protein under HOCl (bleach) stress, discussing how it protects its substrates from both aggregation and ...[more]

PMID: 34017858

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