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

• Published in: FEBS letters Vol. 593; no. 2; pp. 219 - 229
• Main Authors: Cho, Chuloh, Lee, Gun Woong, Hong, Sung H., Kaur, Shubhpreet, Jung, Kwang‐Woo, Jung, Jong‐Hyun, Lim, Sangyong, Chung, Byung Yeoup, Lee, Seung Sik
• Format: Journal Article
• Language: English
• Published: England John Wiley and Sons Inc 01.01.2019
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Cysteine - metabolism; Deinococcus - chemistry; Deinococcus - genetics; Deinococcus - metabolism; Deinococcus radiodurans R1; DR0846; Gene Expression Regulation, Bacterial; Heat-Shock Response; molecular chaperone; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Mutation; Oxidative Stress; peroxidase; Peroxidase - chemistry; Peroxidase - genetics; Peroxidase - metabolism; peroxiredoxin Q; Peroxiredoxins - chemistry; Peroxiredoxins - genetics; Peroxiredoxins - metabolism; Research Letter; Research Letters; molecular chaperone; Deinococcus radiodurans R1; peroxiredoxin Q; DR0846; peroxidase

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 in...