Tags

Type your tag names separated by a space and hit enter

Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function.
Protoplasma. 2017 Jan; 254(1):327-334.P

Abstract

Yeast peroxiredoxin II (yPrxII) is an antioxidant enzyme that plays a protective role against the damage caused by reactive oxygen species (ROS) in Saccharomyces cerevisiae. This enzyme consists of 196 amino acids containing 2-Cys Prx with highly conserved two active cysteine residues at positions 48 and 171. The yPrxII has dual enzymatic functions as a peroxidase and molecular chaperone. To understand the effect of additional cysteine residues on dual functions of yPrxII, S79C-yPrxII and S109C-yPrxII, the substitution of Ser with Cys residue at 79 and 109 positions, respectively, was generated. S109C-yPrxII and S79C-yPrxII showed 3.7- and 2.7-fold higher chaperone and peroxidase activity, respectively, than the wild type (WT). The improvement in enzyme activity was found to be closely associated with structural changes in proteins. S109C-yPrxII had increased β-sheet in its secondary structure and formed high-molecular-weight (HMW) as well as low-molecular-weight (LMW) complexes, but S79C-yPrxII formed only LMW complexes. HMW complexes predominantly exhibited a chaperone function, and LMW complexes showed a peroxidase function. In addition, transgenic yeast cells over-expressing Cys-substituted yPrxII showed greater tolerance against heat and oxidative stress compared to WT-yPrxII.

Authors+Show Affiliations

Research Division for Biotechnology, Advanced Radiation Technology Institute (ARTI), Korea Atomic Energy Research Institute (KAERI), 29 Geumgu-gil, Jeongeup, 56212, Korea. Department of Bioenergy Science and Technology, Chonnam National University, Gwangju, 61186, Republic of Korea.Research Division for Biotechnology, Advanced Radiation Technology Institute (ARTI), Korea Atomic Energy Research Institute (KAERI), 29 Geumgu-gil, Jeongeup, 56212, Korea.Department of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Korea.Department of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Korea.Research Division for Biotechnology, Advanced Radiation Technology Institute (ARTI), Korea Atomic Energy Research Institute (KAERI), 29 Geumgu-gil, Jeongeup, 56212, Korea.Research Division for Biotechnology, Advanced Radiation Technology Institute (ARTI), Korea Atomic Energy Research Institute (KAERI), 29 Geumgu-gil, Jeongeup, 56212, Korea.Department of Molecular Medicine, Lee Gil Ya Cancer and Diabetes Institute, Gachon University, Incheon, 21936, Republic of Korea.Department of Bioenvironmental Chemistry, Chonbuk National University, 567, Baekje-daero, Deokjin-gu, Jeonju, 54896, Korea.Department of Bioenergy Science and Technology, Chonnam National University, Gwangju, 61186, Republic of Korea.Research Division for Biotechnology, Advanced Radiation Technology Institute (ARTI), Korea Atomic Energy Research Institute (KAERI), 29 Geumgu-gil, Jeongeup, 56212, Korea. bychung@kaeri.re.kr.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

26843371

Citation

Hong, Sung Hyun, et al. "Site-specific Mutagenesis of Yeast 2-Cys Peroxiredoxin Improves Heat or Oxidative Stress Tolerance By Enhancing Its Chaperone or Peroxidase Function." Protoplasma, vol. 254, no. 1, 2017, pp. 327-334.
Hong SH, Lee SS, Chung JM, et al. Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function. Protoplasma. 2017;254(1):327-334.
Hong, S. H., Lee, S. S., Chung, J. M., Jung, H. S., Singh, S., Mondal, S., Jang, H. H., Cho, J. Y., Bae, H. J., & Chung, B. Y. (2017). Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function. Protoplasma, 254(1), 327-334. https://doi.org/10.1007/s00709-016-0948-0
Hong SH, et al. Site-specific Mutagenesis of Yeast 2-Cys Peroxiredoxin Improves Heat or Oxidative Stress Tolerance By Enhancing Its Chaperone or Peroxidase Function. Protoplasma. 2017;254(1):327-334. PubMed PMID: 26843371.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function. AU - Hong,Sung Hyun, AU - Lee,Seung Sik, AU - Chung,Jeong Min, AU - Jung,Hyun Suk, AU - Singh,Sudhir, AU - Mondal,Suvendu, AU - Jang,Ho Hee, AU - Cho,Jae-Young, AU - Bae,Hyeun-Jong, AU - Chung,Byung Yeoup, Y1 - 2016/02/03/ PY - 2015/12/09/received PY - 2016/01/25/accepted PY - 2016/2/5/pubmed PY - 2017/3/28/medline PY - 2016/2/5/entrez KW - 2-Cys peroxiredoxin KW - Heat tolerance KW - Molecular chaperone KW - Oxidative stress KW - Peroxidase KW - Site-directed mutagenesis SP - 327 EP - 334 JF - Protoplasma JO - Protoplasma VL - 254 IS - 1 N2 - Yeast peroxiredoxin II (yPrxII) is an antioxidant enzyme that plays a protective role against the damage caused by reactive oxygen species (ROS) in Saccharomyces cerevisiae. This enzyme consists of 196 amino acids containing 2-Cys Prx with highly conserved two active cysteine residues at positions 48 and 171. The yPrxII has dual enzymatic functions as a peroxidase and molecular chaperone. To understand the effect of additional cysteine residues on dual functions of yPrxII, S79C-yPrxII and S109C-yPrxII, the substitution of Ser with Cys residue at 79 and 109 positions, respectively, was generated. S109C-yPrxII and S79C-yPrxII showed 3.7- and 2.7-fold higher chaperone and peroxidase activity, respectively, than the wild type (WT). The improvement in enzyme activity was found to be closely associated with structural changes in proteins. S109C-yPrxII had increased β-sheet in its secondary structure and formed high-molecular-weight (HMW) as well as low-molecular-weight (LMW) complexes, but S79C-yPrxII formed only LMW complexes. HMW complexes predominantly exhibited a chaperone function, and LMW complexes showed a peroxidase function. In addition, transgenic yeast cells over-expressing Cys-substituted yPrxII showed greater tolerance against heat and oxidative stress compared to WT-yPrxII. SN - 1615-6102 UR - https://www.unboundmedicine.com/medline/citation/26843371/Site_specific_mutagenesis_of_yeast_2_Cys_peroxiredoxin_improves_heat_or_oxidative_stress_tolerance_by_enhancing_its_chaperone_or_peroxidase_function_ L2 - https://dx.doi.org/10.1007/s00709-016-0948-0 DB - PRIME DP - Unbound Medicine ER -