The DnaJ-Hsp70-Hsp90 co-chaperon networks in scallops under toxic Alexandrium dinoflagellates exposure

作者：Moli Li, Jie Cheng, Huizhen Wang, Jiaoxia Shi, Xiaogang Xun, Wei Lu, Xubo Wang, Jingjie Hu, Zhenmin Bao, Xiaoli Hu · 发表于：Ecotoxicology and Environmental Safety · 年份：2025 · DOI：10.1016/j.ecoenv.2024.117653 · 被引用次数：6 · 研究领域：Metabolomics and Mass Spectrometry Studies、Mitochondrial Function and Pathology、Redox biology and oxidative stress

Heat shock proteins (Hsps) are highly conserved molecular chaperones with essential roles against biotic and abiotic stressors. A large set of co-chaperons comprising J-domain proteins (DnaJs) regulate the ATPase cycle of Hsp70s with Hsp90s, together constituting a dynamic and functionally versatile network for protein folding/unfolding and regulation. Marine bivalves could accumulate and tolerate paralytic shellfish toxins (PSTs), the well-noted neurotoxins generated during harmful algal blooms. Here, 37 CfDnaJ and 35 PyDnaJ genes were systematically characterized in Zhikong scallop ( Chlamys farreri ) and Yesso scallop ( Patinopecten yessoensis ), the important aquaculture bivalve species in China. After exposure to different PST-producing dinoflagellates, Alexandrium minutum and Alexandrium catenella , diverse DnaJ regulations were presented in scallop hepatopancreas, accumulating incoming PSTs, and kidneys, transforming PSTs into higher toxic analogs. CfDnaJ s ’ up-regulation in kidneys was similar with that in hepatopancreas, while their down-regulation was stronger in kidneys than in hepatopancreas, with CFA.38965.19.DNAJC30 being continuously down-regulated in both tissues of the two algae exposure. Moreover, PyDnaJ s ’ up-regulation was only found in kidneys after A. catenella exposure, and PYE.10799.6.DNAJB1 was down-regulated in both tissues through the experiment. Together with the expression trends and correlation of DnaJ-Hsp70-Hsp90 genes, the organ-, toxin-, and...