Functions of nuclear receptor HR3 during larval-pupal molting in Leptinotarsa decemlineata (Say) revealed by in vivo RNA interference

2015 ◽  
Vol 63 ◽  
pp. 23-33 ◽  
Author(s):  
Wen-Chao Guo ◽  
Xin-Ping Liu ◽  
Kai-Yun Fu ◽  
Ji-Feng Shi ◽  
Feng-Gong Lü ◽  
...  
2002 ◽  
Vol 37 (3) ◽  
pp. 244-253
Author(s):  
Lori J. Kroiss ◽  
Karen L. Broz ◽  
Cindy B. S. Tong ◽  
W. D. Hutchison

Tomatillo (Physalis ixocarpa Brot ex Hornem) resistance to the Colorado potato beetle, Leptinotarsa decemlineata (Say), was evaluated in the laboratory. In vivo assays confirmed that L. decemlineata larvae fed tomatillo leaves had lower weights and survival than larvae fed potato leaves. Larvae fed potato leaves coated with α-tomatine also had lower weights and survival than controls. Larvae were also fed potato leaves coated with tomatillo leaf extracts. These larvae exhibited lower weights but equal survival compared with the controls. Removal of trichome exudates from tomatillo leaves did not affect the detrimental effects of the leaves on larvae. These results confirm the negative effects of tomatillo leaves and α-tomatine on L. decemlineata larval survival and weight. However, HPLC and mass spectrometry results show that α-tomatine was not present in the tomatillo leaf samples we studied. These results suggest that further research is warranted to isolate compounds for further plant resistance research within tomatillo.


2019 ◽  
Vol 109 (05) ◽  
pp. 659-668
Author(s):  
Q.-Y. Xu ◽  
Q.-W. Meng ◽  
P. Deng ◽  
K.-Y. Fu ◽  
W.-C. Guo ◽  
...  

AbstractDietary delivery of bacterially expressed double-stranded RNA (dsRNA) has a great potential for management of Leptinotarsa decemlineata. An important first step is to discover possible RNA-interference (RNAi)-target genes effective against larvae, especially the old larvae. In the present paper, five putative Broad-Complex (BrC) cDNAs (Z1-Z4, and Z6) were identified in L. decemlineata. The expression of the five LdBrC isoforms was suppressed by juvenile hormone signaling, whereas the transcription was upregulated by 20-hydroxyecdysone signaling at the fourth (final) instar larval stage. Feeding of bacterially expressed dsBrC (derived from a common fragment of the five LdBrC variants) in the third- and fourth-instar larvae successfully knocked down the target mRNAs. For the fourth-instar LdBrC RNAi hypomorphs, they had a higher larval mortality compared with the controls. Moreover, most dsBrC-fed beetles did not pupate normally. After removal of the apolysed larval cuticle, a miniature adult was found. The adult head, compound eyes, prothorax, mesothorax, metathorax were found on the dorsal view. Distinct adult cuticle pigmentation was seen on the prothorax. The mouthparts, forelegs, midlegs, and hindlegs could be observed on the ventral view of the miniature adults. For the third-instar LdBrC RNAi specimens, around 20% moribund beetles remained as prepupae and finally died. Therefore, LdBrC is among the most attractive candidate genes for RNAi to control the fourth-instar larvae in L. decemlineata.


2013 ◽  
Vol 451 (3) ◽  
pp. 453-461 ◽  
Author(s):  
Claudia C. S. Chini ◽  
Carlos Escande ◽  
Veronica Nin ◽  
Eduardo N. Chini

The nuclear receptor Rev-erbα has been implicated as a major regulator of the circadian clock and integrates circadian rhythm and metabolism. Rev-erbα controls circadian oscillations of several clock genes and Rev-erbα protein degradation is important for maintenance of the circadian oscillations and also for adipocyte differentiation. Elucidating the mechanisms that regulate Rev-erbα stability is essential for our understanding of these processes. In the present paper, we report that the protein DBC1 (Deleted in Breast Cancer 1) is a novel regulator of Rev-erbα. Rev-erbα and DBC1 interact in cells and in vivo, and DBC1 modulates the Rev-erbα repressor function. Depletion of DBC1 by siRNA (small interfering RNA) in cells or in DBC1-KO (knockout) mice produced a marked decrease in Rev-erbα protein levels, but not in mRNA levels. In contrast, DBC1 overexpression significantly enhanced Rev-erbα protein stability by preventing its ubiquitination and degradation. The regulation of Rev-erbα protein levels and function by DBC1 depends on both the N-terminal and C-terminal domains of DBC1. More importantly, in cells depleted of DBC1, there was a dramatic decrease in circadian oscillations of both Rev-erbα and BMAL1. In summary, our data identify DBC1 as an important regulator of the circadian receptor Rev-erbα and proposes that Rev-erbα could be involved in mediating some of the physiological effects of DBC1.


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