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Insect Mol Biol. 2013 Aug;22(4):366-75. doi: 10.1111/imb.12028. Epub 2013 Apr 19.

Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase.

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  • 1State Key Laboratory of Rice Biology, Key laboratory of Agricultural Entomology, the Ministry of Agriculture of China, Hangzhou, Zhejiang, China.

Abstract

Ceramidases are a group of enzymes that catalyse hydrolysis of ceramides to generate fatty acid and sphingosine. In this study, we report the cloning and characterization of the rice small brown planthopper Laodelphax striatellus neutral ceramidase (nCDase), LsnCer. LsnCer was identified by sequencing the transcriptome of L. striatellus and is a protein of 717 amino acids with a predicted molecular weight of 79.3 kDa. Similarly to other known nCDases, the optimum pH for LsnCer is 8.0 and the optimum temperature is 37 °C for its in vitro activity. LsnCer activity is inhibited by Zn(2+) significantly and Fe(2+) slightly. LsnCer has broad substrate specificity with a preference for ceramides with a medium acyl-chain or a monounsaturated long acyl-chain. Infection with rice strip virus (RSV) or treatment with insecticides significantly increased LsnCer mRNA expression and its enzymatic activity in L. striatellus. These results suggest that LsnCer is a bona fide nCDase that may have a role in adaption of L. striatellus to environmental stresses.

© 2013 Royal Entomological Society.

KEYWORDS:

LsnCer; activity; insecticide; mRNA; nCDase; rice strip virus

PMID:
23601004
[PubMed - indexed for MEDLINE]
PMCID:
PMC3879266
Free PMC Article
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