Tags

Type your tag names separated by a space and hit enter

Novel functions of peroxiredoxin Q from Deinococcus radiodurans R1 as a peroxidase and a molecular chaperone.
FEBS Lett. 2019 01; 593(2):219-229.FL

Abstract

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.

Authors+Show Affiliations

Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea.Jeonju AgroBio-Materials Institute, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea. Department of Radiation Biotechnology and Applied Radioisotope, Korea University of Science and Technology, Daejeon, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea. Department of Radiation Biotechnology and Applied Radioisotope, Korea University of Science and Technology, Daejeon, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea.Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, Korea. Department of Radiation Biotechnology and Applied Radioisotope, Korea University of Science and Technology, Daejeon, Korea.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

30488429

Citation

Cho, Chuloh, et al. "Novel Functions of Peroxiredoxin Q From Deinococcus Radiodurans R1 as a Peroxidase and a Molecular Chaperone." FEBS Letters, vol. 593, no. 2, 2019, pp. 219-229.
Cho C, Lee GW, Hong SH, et al. Novel functions of peroxiredoxin Q from Deinococcus radiodurans R1 as a peroxidase and a molecular chaperone. FEBS Lett. 2019;593(2):219-229.
Cho, C., Lee, G. W., Hong, S. H., Kaur, S., Jung, K. W., Jung, J. H., Lim, S., Chung, B. Y., & Lee, S. S. (2019). Novel functions of peroxiredoxin Q from Deinococcus radiodurans R1 as a peroxidase and a molecular chaperone. FEBS Letters, 593(2), 219-229. https://doi.org/10.1002/1873-3468.13302
Cho C, et al. Novel Functions of Peroxiredoxin Q From Deinococcus Radiodurans R1 as a Peroxidase and a Molecular Chaperone. FEBS Lett. 2019;593(2):219-229. PubMed PMID: 30488429.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Novel functions of peroxiredoxin Q from Deinococcus radiodurans R1 as a peroxidase and a molecular chaperone. AU - Cho,Chuloh, AU - Lee,Gun Woong, AU - Hong,Sung H, AU - Kaur,Shubhpreet, AU - Jung,Kwang-Woo, AU - Jung,Jong-Hyun, AU - Lim,Sangyong, AU - Chung,Byung Yeoup, AU - Lee,Seung Sik, Y1 - 2018/12/11/ PY - 2018/08/07/received PY - 2018/11/14/revised PY - 2018/11/15/accepted PY - 2018/11/30/pubmed PY - 2019/7/23/medline PY - 2018/11/30/entrez KW - DR0846 KW - Deinococcus radiodurans R1 KW - molecular chaperone KW - peroxidase KW - peroxiredoxin Q SP - 219 EP - 229 JF - FEBS letters JO - FEBS Lett VL - 593 IS - 2 N2 - 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. SN - 1873-3468 UR - https://www.unboundmedicine.com/medline/citation/30488429/Novel_functions_of_peroxiredoxin_Q_from_Deinococcus_radiodurans_R1_as_a_peroxidase_and_a_molecular_chaperone_ L2 - https://doi.org/10.1002/1873-3468.13302 DB - PRIME DP - Unbound Medicine ER -