Unknown

Dataset Information

0

Ohr Protects Corynebacterium glutamicum against Organic Hydroperoxide Induced Oxidative Stress.


ABSTRACT: Ohr, a bacterial protein encoded by the Organic Hydroperoxide Resistance (ohr) gene, plays a critical role in resistance to organic hydroperoxides. In the present study, we show that the Cys-based thiol-dependent Ohr of Corynebacterium glutamicum decomposes organic hydroperoxides more efficiently than hydrogen peroxide. Replacement of either of the two Cys residues of Ohr by a Ser residue resulted in drastic loss of activity. The electron donors supporting regeneration of the peroxidase activity of the oxidized Ohr of C. glutamicum were principally lipoylated proteins (LpdA and Lpd/SucB). A ?ohr mutant exhibited significantly decreased resistance to organic hydroperoxides and marked accumulation of reactive oxygen species (ROS) in vivo; protein carbonylation was also enhanced notably. The resistance to hydrogen peroxide also decreased, but protein carbonylation did not rise to any great extent. Together, the results unequivocally show that Ohr is essential for mediation of organic hydroperoxide resistance by C. glutamicum.

SUBMITTER: Si M 

PROVIDER: S-EPMC4486171 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

altmetric image

Publications

Ohr Protects Corynebacterium glutamicum against Organic Hydroperoxide Induced Oxidative Stress.

Si Meiru M   Wang Jianbo J   Xiao Xiao X   Guan Jingyuan J   Zhang Yaoling Y   Ding Wei W   Chaudhry Muhammad Tausif MT   Wang Yao Y   Shen Xihui X  

PloS one 20150629 6


Ohr, a bacterial protein encoded by the Organic Hydroperoxide Resistance (ohr) gene, plays a critical role in resistance to organic hydroperoxides. In the present study, we show that the Cys-based thiol-dependent Ohr of Corynebacterium glutamicum decomposes organic hydroperoxides more efficiently than hydrogen peroxide. Replacement of either of the two Cys residues of Ohr by a Ser residue resulted in drastic loss of activity. The electron donors supporting regeneration of the peroxidase activity  ...[more]

Similar Datasets

| S-EPMC4052852 | biostudies-other
| S-EPMC127688 | biostudies-literature
| S-EPMC107214 | biostudies-literature
| S-EPMC1386026 | biostudies-other
| S-EPMC7599745 | biostudies-literature
| S-EPMC5811025 | biostudies-literature
| S-EPMC2903379 | biostudies-literature
| S-EPMC95027 | biostudies-literature
| S-EPMC7906806 | biostudies-literature
2013-02-01 | E-MEXP-3523 | biostudies-arrayexpress