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Identification and biochemical characterization of L aodelphax striatellus neutral ceramidase
Author(s) -
Zhou Y.,
Lin X.W.,
Zhang Y.R.,
Huang Y.J.,
Zhang C.H.,
Yang Q.,
Li H.Y.,
Yuan J.Q.,
Cheng J.A.,
Xu R.,
Mao C.,
Zhu Z.R.
Publication year - 2013
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12028
Subject(s) - biology , biochemistry , sphingolipid , enzyme , transcriptome , cloning (programming) , brown planthopper , sphingosine , hydrolysis , fatty acid , microbiology and biotechnology , gene , gene expression , receptor , computer science , programming language
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 L aodelphax 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 nCD ases, 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.
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