Cloning of heat shock protein genes from the brown planthopper,Nilaparvata lugens, and the small brown planthopper,Laodelphax striatellus, and their expression in relation to thermal stress

2008 ◽  
Vol 15 (5) ◽  
pp. 415-422 ◽  
Author(s):  
Dong Hun Kim ◽  
Sang-Chul Lee ◽  
Do-Yeon Kwak ◽  
Kyeong-Yeoll Lee
Genes ◽  
2020 ◽  
Vol 11 (9) ◽  
pp. 1074
Author(s):  
Xuan Chen ◽  
Ze-Dong Li ◽  
Yi-Ting Dai ◽  
Ming-Xing Jiang ◽  
Chuan-Xi Zhang

Hsp90 (heat shock protein 90) chaperone machinery is considered to be a key regulator of proteostasis under both physiological and stress growth conditions in eukaryotic cells. The high conservation of both the sequence and function of Hsp90 allows for the utilization of various species to explore new phenotypes and mechanisms. In this study, three Hsp90 homologs were identified in the brown planthopper (BPH), Nilaparvata lugens: cytosolic NlHsp90, endoplasmic reticulum (ER) NlGRP94 and mitochondrial NlTRAP1. Sequence analysis and phylogenetic construction showed that these proteins belonged to distinct classes consistent with the predicted localization and suggested an evolutionary relationship between NlTRAP1 and bacterial HtpG (high-temperature protein G). Temporospatial expression analyses showed that NlHsp90 was inducible under heat stress throughout the developmental stage, while NlGRP94 was only induced at the egg stage. All three genes had a significantly high transcript level in the ovary. The RNA interference-mediated knockdown of NlHsp90 its essential role in nymph development and oogenesis under physiological conditions. NlGRP94 was also required during the early developmental stage and played a crucial role in oogenesis, fecundity and late embryogenesis. Notably, we first found that NlHsp90 and NlGRP94 were likely involved in the cuticle structure of female BPH. Together, our research revealed multifunctional roles of Hsp90s in the BPH.


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