Novel functions of peroxiredoxin Q from Deinococcus radiodurans R1 as a peroxidase and a molecular chaperone

FEBS Letters

article

Chuloh Cho¹  Gun Woong Lee²  Sung H. Hong¹  Shubhpreet Kaur¹  Kwang-Woo Jung¹  Jong-Hyun Jung¹  Sangyong Lim¹  Byung Yeoup Chung¹  Seung Sik Lee¹ 

[1]Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute

[2]Jeonju AgroBio-Materials Institute

[3]Department of Radiation Biotechnology and Applied Radioisotope, Korea University of Science and Technology

关键词: Deinococcus radiodurans R1;    DR0846;    molecular chaperone;    peroxidase;    peroxiredoxin Q;    ;   

DOI  :  10.1002/1873-3468.13302

来源: John Wiley & Sons Ltd.

【 摘 要 】

Deinococcus radiodurans R1 is extremely resistant to ionizing radiation and oxidative stress. In this study, we characterized DR0846, a candidate peroxiredoxin in D. radiodurans. DR0846 is a peroxiredoxin Q containing two conserved cysteine residues. DR0846 exists mainly in monomeric form with an intramolecular disulfide bond between the two cysteine residues. We found that DR0846 functions as a molecular chaperone as well as a peroxidase. A mutational analysis indicates that the two cysteine residues are essential for enzymatic activity. A double-deletion mutant lacking DR0846 and catalase DR1998 exhibits decreased oxidative and heat shock stress tolerance with respect to the single mutants or the wild-type cells. These results suggest that DR0846 contributes to resistance against oxidative and heat stresses in D. radiodurans.

【 授权许可】

Unknown