A 1-Cys Peroxiredoxin from a Thermophilic Archaeon Moonlights as a Molecular Chaperone to Protect Protein and DNA against Stress-Induced Damage.
Peroxiredoxins (Prxs) act against hydrogen peroxide (H2O2), organic peroxides, and peroxynitrite. Thermococcus kodakaraensis KOD1, an anaerobic archaeon, contains many antioxidant proteins, including three Prxs (Tk0537, Tk0815, and Tk1055). Only Tk0537 has been found to be induced in response to heat, osmotic, and oxidative stress. Tk0537 was found to belong to a 1-Cys Prx6 subfamily based on sequence analysis and was named 1-Cys TkPrx. Using gel filtration chromatography, electron microscopy, and blue-native polyacrylamide gel electrophoresis, we observed that 1-Cys TkPrx exhibits oligomeric forms with reduced peroxide reductase activity as well as decameric and dodecameric forms that can act as molecular chaperones by protecting both proteins and DNA from oxidative stress. Mutational analysis showed that a cysteine residue at the N-terminus (Cys46) was responsible for the peroxide reductase activity, and cysteine residues at the C-terminus (Cys205 and Cys211) were important for oligomerization. Based on our results, we propose that interconversion between different oligomers is important for regulating the different functions of 1-Cys TkPrx.
Division of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea; Division of Electron Microscopic Research, Korea Basic Science Institute, Daejeon, Korea.
Sangmin
S
Lee
Division of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea; Department of Life Sciences, Chung-Ang University, Seoul, Korea.
Baolei
B
Jia
College of Plant Sciences, Jilin University, Changchun, China.
Jinliang
J
Liu
Division of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea.
Bang Phuong
BP
Pham
Division of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea.
Jae Myeong
JM
Kwak
College of Pharmaceutical Sciences, Wenzhou Medical University, Wenzhou, China.
Yuan Hu
YH
Xuan
Division of Applied Life Sciences and Research Institute of Natural Science, Gyeongsang National University, Jinju, Korea.
Gang-Won
GW
Cheong
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D003001:Cloning, Molecular; D004249:DNA Damage; D004269:DNA, Bacterial / Q000378:metabolism*; D017665:Hydroxyl Radical / Q000378:metabolism; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D050505:Mutant Proteins / Q000737:chemistry; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism; D054464:Peroxiredoxins / Q000737:chemistry / Q000378:metabolism*; D017354:Point Mutation; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D020539:Sequence Analysis, Protein; D013312:Stress, Physiological; D013696:Temperature; D019712:Thermococcus / Q000378:metabolism*; D015854:Up-Regulation
D019843:Archaeal Proteins; D004269:DNA, Bacterial; D018832:Molecular Chaperones; D050505:Mutant Proteins; D011994:Recombinant Proteins; D017665:Hydroxyl Radical; D054464:Peroxiredoxins; D009195:Peroxidase