Characterization of Arabidopsis secretory phospholipase A2‐γ cDNA and its enzymatic properties

FEBS Letters

Ryu, Stephen B.¹  Kim, Hae Jin²  Lee, Hyoung Yool¹  Bahn, Sung Chul²  Shin, Jeong Sheop² 

[1] Kumho Life and Environmental Science Laboratory, Gwangju 500-712, South Korea;School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, South Korea

关键词: Secretory phospholipase A2;    AtsPLA2-γ;    Phospholipid;    Lysophospholipid;    Phosphatidylethanolamine;    Phosphatidylcholine;    AtsPLA2-γ;    Arabidopsis thaliana secretory phospholipase A2-γ;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    LysoPC;    lysophosphatidylcholine;    LysoPE;    lysophosphatidylethanolamine;    FFA;    free fatty acid;    JA;    jasmonic acid;    LA;    linolenic acid;    PLD;    phospholipase D;   

DOI  :  10.1016/S0014-5793(03)00982-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Plant secretory phospholipases A₂ (sPLA₂s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA₂ genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A₂-γ (AtsPLA₂-γ) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA₂-γ showed maximal enzyme activity at pH 8.0, and required Ca²⁺ for activity. Moreover, AtsPLA₂-γ showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA₂-γ was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA₂-γ is secreted into the intercellular space.

【 授权许可】

Unknown