Abstract
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.
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This work was supported by the Special Fund for Fisheries-Scientific Research (A201300B03), the Special Scientific Research Funds for Central Non-profit Institutes (2015YD05, 2014TS12), the Guangdong Provincial Science and Technology Program (2013B040402016, 2014A020208039) and the Guangdong Province Marine Fishery Science and Technology and Industrial Development of Special Scientific and Technological Research and Development Projects (A201501A11).
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Shi, J., Fu, M., Zhao, C. et al. Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon . Cell Stress and Chaperones 21, 295–312 (2016). https://doi.org/10.1007/s12192-015-0660-6
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DOI: https://doi.org/10.1007/s12192-015-0660-6