Journal
CELL STRESS & CHAPERONES
Volume 19, Issue 5, Pages 623-633Publisher
SPRINGER
DOI: 10.1007/s12192-013-0487-y
Keywords
HSP90; Heat stress; Development; Reproduction; Lifespan; Tribolium castaneum
Categories
Funding
- National Natural Science Foundation of China [31172146]
- Natural Science Foundation of Jiangsu Province, China [BK2011785]
- Key Project of Natural Science Foundation of the Jiangsu Higher Education Institutions of China [10KJA180023]
- PAPD of Jiangsu Higher Education Institutions
- Excellent Talent Project of Nanjing Normal University of China
- graduate innovation research projects of Jiangsu colleges and universities
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Heat-shock protein 90 (HSP90) is a highly conserved molecular chaperone found in all species except for Archaea, which is required not only for stress tolerance but also for normal development. Recently, it was reported that HSP83, one member of the cytosolic HSP90 family, contributes to oogenesis and responds to heat resistance in Tribolium castaneum. Here, a novel ER-based HSP90 gene, Tchsp90, has been identified in T. castaneum. Phylogenetic analysis showed that hsp90s and hsp83s evolved separately from a common ancestor but that hsp90s originated earlier. Quantitative real-time polymerase chain reaction illustrated that Tchsp90 is expressed in all developmental stages and is highly expressed at early pupa and late adult stages. Tchsp90 was upregulated in response to heat stress but not to cold stress. Laval RNAi revealed that Tchsp90 is important for larval/pupal development. Meanwhile, parental RNAi indicated that it completely inhibited female fecundity and partially inhibited male fertility once Tchsp90 was knocked down and that it will further shorten the lifespan of T. castaneum. These results suggest that Tchsp90 is essential for development, lifespan, and reproduction in T. castaneum in addition to its response to heat stress.
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