文献类型：期刊文献

英文题名：Peroxiredoxin System of Aspergillus nidulans Resists Inactivation by High Concentration of Hydrogen Peroxide-Mediated Oxidative Stress

作者：Xia, Yang[1];Yu, Haijun[1];Zhou, Zhemin[2];Takaya, Naoki[3];Zhou, Shengmin[1];Wang, Ping[1]

机构：[1]East China Univ Sci & Technol, Sch Biotechnol, Biomed Nanotechnol Ctr, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Jiangnan Univ, Sch Biotechnol, Wuxi 214122, Jiangsu, Peoples R China;[3]Univ Tsukuba, Grad Sch Life & Environm Sci, Tsukuba, Ibaraki 3050006, Japan

年份：2018

卷号：28

期号：1

起止页码：145

外文期刊名：JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000423604600017)】；

基金：This work was sponsored by the National Natural Science Foundation of China (21672065, 21636003, and 31471659), the Shanghai Pujiang Program (16PJ1402500), and the National Special Fund for State Key Laboratory of Bioreactor Engineering (Grant No. 2060204).

语种：英文

外文关键词：Peroxiredoxin; filamentous fungus; thioredoxin; thioredoxin reductase; oxidative stress; hydrogen peroxide

摘要：Most eukaryotic peroxiredoxins (Prxs) are readily inactivated by a high concentration of hydrogen peroxide (H2O2) during catalysis owing to their "GGLG" and "YF" motifs. However, such oxidative stress sensitive motifs were not found in the previously identified filamentous fungal Prxs. Additionally, the information on filamentous fungal Prxs is limited and fragmentary. Herein, we cloned and gained insight into Aspergillus nidulans Prx (An.PrxA) in the aspects of protein properties, catalysis characteristics, and especially H2O2 tolerability. Our results indicated that An. PrxA belongs to the newly defined family of typical 2-Cys Prxs with a marked characteristic that the "resolving" cysteine (C-R) is invertedly located preceding the "peroxidatic" cysteine (C-P) in amino acid sequences. The inverted arrangement of C-R and C-P can only be found among some yeast, bacterial, and filamentous fungal deduced Prxs. The most surprising characteristic of An. PrxA is its extraordinary ability to resist inactivation by extremely high concentrations of H2O2, even that approaching 600 mM. By screening the H2O2-inactivation effects on the components of Prx systems, including Trx, Trx reductase (TrxR), and Prx, we ultimately determined that it is the robust filamentous fungal TrxR rather than Trx and Prx that is responsible for the extreme H2O2 tolerence of the An. PrxA system. This is the first investigation on the effect of the electron donor partner in the H2O2 tolerability of the Prx system.