Shi Jinxuan, Fu Mingjun, Zhao Chao, Zhou Falin, Yang Qibin, Qiu Lihua
South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, 510300, China.
College of Aqua-life Science and Technology, Shanghai Ocean University, Shanghai, 201306, China.
Cell Stress Chaperones. 2016 Mar;21(2):295-312. doi: 10.1007/s12192-015-0660-6. Epub 2015 Dec 4.
Heat shock proteins (Hsps) are a class of highly conserved proteins produced in virtually all living organisms from bacteria to humans. Hsp60 and Hsp10, the most important mitochondrial chaperones, participate in environmental stress responses. In this study, the full-length complementary DNAs (cDNAs) of Hsp60 (PmHsp60) and Hsp10 (PmHsp10) were cloned from Penaeus monodon. Sequence analysis showed that PmHsp60 and PmHsp10 encoded polypeptides of 578 and 102 amino acids, respectively. The expression profiles of PmHsp60 and PmHsp10 were detected in the gills and hepatopancreas of the shrimps under pH challenge, osmotic stress, and heavy metal exposure, and results suggested that PmHsp60 and PmHsp10 were involved in the responses to these stimuli. ATPase and chaperone activity assay indicated that PmHsp60 could slow down protein denaturation and that Hsp60/Hsp10 may be combined to produce a chaperone complex with effective chaperone and ATPase activities. Overall, this study provides useful information to help further understand the functional mechanisms of the environmental stress responses of Hsp60 and Hsp10 in shrimp.
热休克蛋白（Hsps）是一类高度保守的蛋白质，几乎在从细菌到人类的所有生物中都有产生。Hsp60和Hsp10是最重要的线粒体伴侣蛋白，参与环境应激反应。在本研究中，从斑节对虾中克隆了Hsp60（PmHsp60）和Hsp10（PmHsp10）的全长互补DNA（cDNA）。序列分析表明，PmHsp60和PmHsp10分别编码578和102个氨基酸的多肽。在pH值挑战、渗透应激和重金属暴露条件下，检测了斑节对虾鳃和肝胰腺中PmHsp60和PmHsp10的表达谱，结果表明PmHsp60和PmHsp10参与了对这些刺激的反应。ATP酶和伴侣活性测定表明，PmHsp60可以减缓蛋白质变性，并且Hsp60/Hsp10可能结合形成具有有效伴侣和ATP酶活性的伴侣复合物。总体而言，本研究提供了有用信息，有助于进一步了解对虾中Hsp60和Hsp10环境应激反应的功能机制。
