Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase

文献类型: 外文期刊

第一作者: Zhou, Y.

作者: Zhou, Y.;Lin, X. -W.;Zhang, Y. -R.;Huang, Y. -J.;Zhang, C. -H.;Yang, Q.;Yuan, J. -Q.;Cheng, J. -A.;Zhu, Z. -R.;Zhou, Y.;Lin, X. -W.;Zhang, Y. -R.;Huang, Y. -J.;Zhang, C. -H.;Yang, Q.;Yuan, J. -Q.;Cheng, J. -A.;Zhu, Z. -R.;Zhou, Y.;Xu, R.;Mao, C.;Li, H. -Y.;Yang, Q.

作者机构:

关键词: nCDase;LsnCer;activity;mRNA;rice strip virus;insecticide

期刊名称:INSECT MOLECULAR BIOLOGY ( 影响因子:3.585; 五年影响因子:3.215 )

ISSN: 0962-1075

年卷期: 2013 年 22 卷 4 期

页码:

收录情况: SCI

摘要: 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 degrees C for its in vitro activity. LsnCer activity is inhibited by Zn2+ significantly and Fe2+ 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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