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Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis

Rieske iron-sulfur protein (RISP) is a key protein subunit of mitochondrial complex III which plays an important role in the respiratory electron transport chain. The complete cDNA of RISP was cloned from Spodoptera exigua by real time quantitative PCR and rapid-amplification of cDNA ends (RACE) tec...

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Autores principales: Shi, Song, Zuo, Hongliang, Gao, Lu, Yi, Xin, Zhong, Guohua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5977497/
https://www.ncbi.nlm.nih.gov/pubmed/29881355
http://dx.doi.org/10.3389/fphys.2018.00575
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author Shi, Song
Zuo, Hongliang
Gao, Lu
Yi, Xin
Zhong, Guohua
author_facet Shi, Song
Zuo, Hongliang
Gao, Lu
Yi, Xin
Zhong, Guohua
author_sort Shi, Song
collection PubMed
description Rieske iron-sulfur protein (RISP) is a key protein subunit of mitochondrial complex III which plays an important role in the respiratory electron transport chain. The complete cDNA of RISP was cloned from Spodoptera exigua by real time quantitative PCR and rapid-amplification of cDNA ends (RACE) technology and named as SeRISP (GenBank Accession Number: JN992290). Multiple alignments and the creation of a phylogenetic tree revealed that RISPs are highly conserved among different insects, and the highly conserved region of RISPs is mainly located at the C-terminal which serves as the functional domain. Expression pattern analysis demonstrated that SeRISP is expressed in all developmental stages of S. exigua; the expression levels increased during larval growth, remained stable during development from fourth instar to pupa and reached a peak in the adult. In addition, SeRISP was significantly suppressed at both the mRNA and protein levels by feeding the instar stage with dsRNA; levels of suppression increased with increasing dsRNA concentration and continuous treatment time. The silencing of SeRISP in larvae led to the significant inhibition of ATP synthesis and larval growth, which could result in energy reserve deficiency in pupae and the suppression of fecundity and hatchability in adults. Our findings confirmed that it is possible to silence target genes in S. exigua by simple dsRNA feeding, and provided evidence of the essential role of RISP in the process of ATP synthesis, growth and reproduction.
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spelling pubmed-59774972018-06-07 Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis Shi, Song Zuo, Hongliang Gao, Lu Yi, Xin Zhong, Guohua Front Physiol Physiology Rieske iron-sulfur protein (RISP) is a key protein subunit of mitochondrial complex III which plays an important role in the respiratory electron transport chain. The complete cDNA of RISP was cloned from Spodoptera exigua by real time quantitative PCR and rapid-amplification of cDNA ends (RACE) technology and named as SeRISP (GenBank Accession Number: JN992290). Multiple alignments and the creation of a phylogenetic tree revealed that RISPs are highly conserved among different insects, and the highly conserved region of RISPs is mainly located at the C-terminal which serves as the functional domain. Expression pattern analysis demonstrated that SeRISP is expressed in all developmental stages of S. exigua; the expression levels increased during larval growth, remained stable during development from fourth instar to pupa and reached a peak in the adult. In addition, SeRISP was significantly suppressed at both the mRNA and protein levels by feeding the instar stage with dsRNA; levels of suppression increased with increasing dsRNA concentration and continuous treatment time. The silencing of SeRISP in larvae led to the significant inhibition of ATP synthesis and larval growth, which could result in energy reserve deficiency in pupae and the suppression of fecundity and hatchability in adults. Our findings confirmed that it is possible to silence target genes in S. exigua by simple dsRNA feeding, and provided evidence of the essential role of RISP in the process of ATP synthesis, growth and reproduction. Frontiers Media S.A. 2018-05-24 /pmc/articles/PMC5977497/ /pubmed/29881355 http://dx.doi.org/10.3389/fphys.2018.00575 Text en Copyright © 2018 Shi, Zuo, Gao, Yi and Zhong. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Shi, Song
Zuo, Hongliang
Gao, Lu
Yi, Xin
Zhong, Guohua
Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis
title Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis
title_full Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis
title_fullStr Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis
title_full_unstemmed Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis
title_short Silencing of Rieske Iron-Sulfur Protein Impacts Upon the Development and Reproduction of Spodoptera exigua by Regulating ATP Synthesis
title_sort silencing of rieske iron-sulfur protein impacts upon the development and reproduction of spodoptera exigua by regulating atp synthesis
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5977497/
https://www.ncbi.nlm.nih.gov/pubmed/29881355
http://dx.doi.org/10.3389/fphys.2018.00575
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