Abstract
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.
Highlights
Hsp90, with an approximate molecular weight of 90 kDa, is a highly ubiquitous molecular chaperone, which accounts for 1–2% of cellular proteins under normal growth conditions [1]
NlGRP94 was required during the early developmental stage and played a crucial role in oogenesis, fecundity and late embryogenesis
We first found that NlHsp90 and NlGRP94 were likely involved in the cuticle structure of female brown planthopper (BPH)
Summary
Hsp (heat shock protein 90), with an approximate molecular weight of 90 kDa, is a highly ubiquitous molecular chaperone, which accounts for 1–2% of cellular proteins under normal growth conditions [1]. Hsp protein family members stabilize, activate and regulate target proteins together with a cohort of cochaperones under both physiological and stress conditions, maintaining proteostasis and cellular homeostasis [2,3]. Apart from molecular weight, further classification of Hsp can be based on subcellular localization [4]. Most bacteria have one homolog of Hsp, known as HtpG (high-temperature protein G). Higher eukaryotes harbor up to four distinct homologs of Hsp: Hsp in the cytosol, GRP94 (94 kDa glucose-regulated protein) in the endoplasmic reticulum (ER), mitochondrial TRAP1
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