Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions.

ABSTRACT: Peroxiredoxins (Prxs) are ubiquitous antioxidants utilizing a reactive cysteine for peroxide reduction and acting as a molecular chaperone under various stress conditions. Besides other stimulating factors, oxidative- and heat stress conditions trigger their ATP-independent chaperoning function. So far, many studies were intended to reveal the chaperoning mechanisms of the so-called sensitive Prxs of eukaryotes, which are susceptible to inactivation by over-oxidation of its reactive cysteine during H₂O₂ reduction. In contrast, the chaperone mechanisms of bacterial Prxs, which are mostly robust against inactivation by over-oxidation, are not well understood. Herein, comprehensive biochemical and biophysical studies demonstrate that the Escherichia coli alkyl hydroperox

SUBMITTER: Kamariah N 

PROVIDER: S-EPMC6147784 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature