Methionine Redox Homeostasis in Protein Quality Control

Bacteria live in different environments and are subject to a wide variety of fluctuating conditions. During evolution, they acquired sophisticated systems dedicated to maintaining protein structure and function, especially during oxidative stress. Under such conditions, methionine residues are converted into methionine sulfoxide (Met-O) which can alter protein function. In this review, we focus on the role in protein quality control of methionine sulfoxide reductases (Msr) which repair oxidatively protein-bound Met-O. We discuss our current understanding of the importance of Msr systems in rescuing protein function under oxidative stress and their ability to work in coordination with chaperone networks. Moreover, we highlight that bacterial chaperones, like GroEL or SurA, are also targeted by oxidative stress and under the surveillance of Msr. Therefore, integration of methionine redox homeostasis in protein quality control during oxidative stress gives a complete picture of this bacterial adaptive mechanism.

Automated summary

Bacteria have evolved sophisticated systems, such as methionine sulfoxide reductases (Msr), to maintain protein structure and function during oxidative stress. Msr repair oxidatively protein-bound methionine residues (Met-O) and work in coordination with chaperone networks to rescue protein function. Integration of methionine redox homeostasis in protein quality control gives a complete picture of bacterial adaptive mechanism during oxidative stress.