CAS Key Laboratory of Marine Ecology and Environmental Sciences, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China.
Laboratory of Marine Ecology and Environmental Science, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266237, China.
Int J Mol Sci. 2021 Oct 13;22(20):11054. doi: 10.3390/ijms222011054.
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone functioning in cellular structural folding and conformational integrity maintenance and thus plays vital roles in a variety of biological processes. However, many aspects of these functions and processes remain to be fully elucidated, particularly for non-model organisms. Dinoflagellates are a group of eukaryotes that are exceedingly important in primary production and are responsible for the most harmful algal blooms (HABs) in aquatic ecosystems. The success of dinoflagellates in dominating the plankton community is undoubtedly pertinent to their remarkable adaptive strategies, characteristic of resting cyst production and broad tolerance to stresses of temperature and others. Therefore, this study was conducted to examine the putative roles of in the acclimation to temperature stress and life stage alterations of dinoflagellates. Firstly, we isolated the full-length cDNA of an Hsp90 gene () via RACE from the cosmopolitan HAB species and tracked its transcriptions in response to varied scenarios via real-time qPCR. The results indicated that displayed significant mRNA augment patterns, escalating during 180-min treatments, when the cells were exposed to elevated and lowered temperatures. Secondly, we observed prominently elevated transcriptions in the cysts that were stored at the cold and dark conditions compared to those in newly formed resting cysts and vegetative cells. Finally, and perhaps most importantly, we identified 29 entries of -encoding genes with complete coding regions from a dinoflagellate-specific environmental cDNA library generated from marine sediment assemblages. The observed active transcription of these genes in sediment-buried resting cysts was fully supported by the qPCR results for the cold-stored resting cysts of . expressions in both laboratory-raised and field-collected cysts collectively highlighted the possible involvement and engagement of Hsp90 chaperones in the resting stage persistence of dinoflagellates.
热休克蛋白 90(Hsp90)是一种高度保守的分子伴侣,在细胞结构折叠和构象完整性维持中发挥作用,因此在各种生物过程中发挥着至关重要的作用。然而,这些功能和过程的许多方面仍有待充分阐明,特别是对于非模式生物。甲藻是一类真核生物,在初级生产中极为重要,是水生生态系统中最有害的藻华(HABs)的罪魁祸首。甲藻在浮游生物群落中占主导地位的成功无疑与其显著的适应策略有关,其特征是休眠囊的产生和对温度和其他压力的广泛耐受。因此,本研究旨在研究 Hsp90 在甲藻对温度胁迫的适应和生活史变化中的可能作用。首先,我们通过 RACE 从世界性赤潮物种中分离出全长 cDNA,并通过实时 qPCR 跟踪其转录以响应各种情况。结果表明,在细胞暴露于高温和低温处理 180 分钟时, 显示出显著的 mRNA 增加模式。其次,我们观察到在储存于寒冷和黑暗条件下的休眠囊中, 转录明显升高,与新形成的休眠囊和营养细胞相比。最后,也许最重要的是,我们从海洋沉积物组合中生成的甲藻特异性环境 cDNA 文库中鉴定出 29 个具有完整编码区的 -编码基因。qPCR 结果充分支持了这些基因在埋藏于沉积物中的休眠囊中活跃转录,这表明 Hsp90 伴侣蛋白可能参与和参与了甲藻休眠期的持续。