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Molecular cloning and characterization of a ryanodine receptor gene in brown planthopper ( BPH ), Nilaparvata lugens (Stål)
Author(s) -
Wang Jian,
Xie Zhijuan,
Gao Jingkun,
Liu Yaping,
Wang Wenlong,
Huang Li,
Wang Jianjun
Publication year - 2014
Publication title -
pest management science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.296
H-Index - 125
eISSN - 1526-4998
pISSN - 1526-498X
DOI - 10.1002/ps.3616
Subject(s) - ryanodine receptor , brown planthopper , biology , delphacidae , alternative splicing , gene , genetics , rna splicing , open reading frame , exon , microbiology and biotechnology , peptide sequence , receptor , botany , pest analysis , rna , homoptera
BACKGROUND Ryanodine receptors (RyRs) are a distinct class of intracellular calcium (Ca 2+ ) release channel. The recent discovery of diamide insecticides has prompted studies on insect RyRs. However, information about the structure and function of insect RyRs is still limited. In this study, we isolated and characterized a full‐length RyR cDNA (named NlRyR ) from the brown planthopper, Nilaparvata lugens (Stål) (Homoptera: Delphacidae), a serious rice pest throughout Asia . RESULTS The composite NlRyR gene contains an open reading frame of 15 423 bp encoding a protein of 5140 amino acid residues, which shares high sequence identity (78–81%) with other insect homologues, except for two regions (IDR1: 4379–4732; IDR2: 1307–1529) with markedly low identity (44–48 and 38–41%, respectively). All hallmarks of the RyR proteins are conserved in the NlRyR protein, including the RyR domain as well as mannosyltransferase, IP 3 R and RyR (pfam02815) (MIR) and RyR and IP 3 R homology (pfam01365) (RIH) domains. Expression analysis of NlRyR revealed significant differences in mRNA expression levels among N. lugens developmental stages. Furthermore, three alternative splicing sites were identified in NlRyR , one of which forms the mutually exclusive exons A/B and is conserved in various insect species. Diagnostic PCR assays showed that the splice variant containing exon A was predominantly detected in all developmental stages . CONCLUSION NlRyR may play an important role in the control of developmental processes of N. lugens . Alternative splicing may generate the functional diversity of NlRyR . The results provided the basis for further structural and functional characterization of NlRyR . © 2013 Society of Chemical Industry