Myo‐inositol‐1‐phosphate synthase (Ino‐1) functions as a protection mechanism in Corynebacterium glutamicum under oxidative stress

• Main Authors: Can Chen, Keqi Chen, Tao Su, Bing Zhang, Guizhi Li, Junfeng Pan, Meiru Si
• Format: Article
• Language: English
• Published: Wiley 2019-05-01
• Series: MicrobiologyOpen
• Subjects: Corynebacterium glutamicum; Myo‐inositol‐1‐phosphate synthase (Ino‐1); oxidative stress; protein carbonylation
• Online Access: https://doi.org/10.1002/mbo3.721

Abstract Reactive oxygen species (ROS) generated in aerobic metabolism and oxidative stress lead to macromolecules damage, such as to proteins, lipids, and DNA, which can be eliminated by the redox buffer mycothiol (AcCys‐GlcN‐Ins, MSH). Myo‐inositol‐phosphate synthase (Ino‐1) catalyzes the first committed step in the synthesis of MSH, thus playing a critical role in the growth of the organism. Although Ino‐1s have been systematically studied in eukaryotes, their physiological and biochemical functions remain largely unknown in bacteria. In this study, we report that Ino‐1 plays an important role in oxidative stress resistance in the gram‐positive Actinobacteria Corynebacterium glutamicum. Deletion of the ino‐1 gene resulted in a decrease in cell viability, an increase in ROS production, and the aggravation of protein carbonylation levels under various stress conditions. The physiological roles of Ino‐1 in the resistance to oxidative stresses were corroborated by the absence of MSH in the Δino‐1 mutant. In addition, we found that the homologous expression of Ino‐1 in C. glutamicum yielded a functionally active protein, while when expressed in Escherichia coliBL21(DE3), it lacked measurable activity. An examination of the molecular mass (Mr) suggested that Ino‐1 expressed in E. coliBL21(DE3) was not folded in a catalytically competent conformation. Together, the results unequivocally showed that Ino‐1 was important for the mediation of oxidative resistance by C. glutamicum.