文献类型：期刊文献

英文题名：Peroxiredoxin PrxA and thioredoxin TrxA mediate the redox signal to the transcription factor NapA in the fungus Aspergillus nidulans

作者：Liu, Feiyun[1];Guo, Lingyan[1];Luo, Yiqing[1];Li, Jingyi[1];Zhou, Yao[1];Wang, Jing[1];Huang, Xiaofei[1];Tan, Xinyu[1];Fu, Mingxin[1];Yu, Bingzi[1];Gao, Yan[1];Liu, Renning[1];Takaya, Naoki[3];Zhou, Shengmin[1,2]

机构：[1]East China Univ Sci & Technol, Sch Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Peking Univ, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China;[3]Univ Tsukuba, Fac Life & Environm Sci, Tsukuba, Ibaraki 3058572, Japan

年份：2025

卷号：310

外文期刊名：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

收录：;EI(收录号：20251718314573);WOS:【SCI-EXPANDED(收录号:WOS:001482464100001)】；

基金：This study was supported by the National Natural Science Foundation of China (22077032 and 21672065) , the State Key Laboratory of Natural and Biomimetic Drugs (K202415) .

语种：英文

外文关键词：Peroxiredoxin; Thioredoxin; H 2 O 2 signal

摘要：Ap-1-like transcription factors play a crucial role in regulating antioxidant gene expression and protecting cells from oxidative stress. Extensive research on redox regulation in Saccharomyces cerevisiae and Schizosaccharomyces pombe has revealed notable differences in their mechanisms. However, it remains unclear whether filamentous fungi share similarities with either yeast system or employ a distinct signaling strategy. To address this, we investigated the redox signal relay in Aspergillus nidulans, focusing on how peroxiredoxin PrxA and thioredoxin TrxA modulate the activity of the Ap-1-like transcription factor NapA. We demonstrate that PrxA is essential for NapA activation, transmitting the H2O2 signal through a disulfide bond between its peroxidatic and resolving cysteines to NapA's Cys558, which subsequently forms an intramolecular disulfide bond with Cys404. Furthermore, we reveal that TrxA, rather than Txl1, is responsible for reducing and inactivating NapA by direct interaction in both the cytoplasm and nucleus, utilizing its own catalytic cysteine residues. These findings establish a mechanistic framework for NapA activation and reduction, providing new insights into oxidative stress responses in filamentous fungi and their divergence from yeast systems.