N‐terminal EF‐hand‐like domain is required for phosphoinositide‐specific phospholipase C activity in Arabidopsis thaliana

FEBS Letters

Pical, Christophe¹  Sommarin, Marianne¹  Otterhag, Lotta¹ 

[1] Department of Plant Biochemistry, Lund University, P.O. Box 117, SE-221 00 Lund, Sweden

关键词: Phosphoinositide-specific phospholipase C;    Phosphoinositide;    EF-hand;    Plasma membrane;    Arabidopsis thaliana;    PI-PLC;    phosphoinositide-specific phospholipase C;    PtdIns;    phosphatidylinositol;    PtdIns(4;    5)P2;    phosphatidylinositol 4;    5-bisphosphate;    PH;    pleckstrin homology;   

DOI  :  10.1016/S0014-5793(01)02453-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphoinositide-specific phospholipase C's (PI-PLCs) are ubiquitous in eukaryotes, from plants to animals, and catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate into the two second messengers inositol 1,4,5-trisphosphate and diacylglycerol. In animals, four distinct subfamilies of PI-PLCs have been identified, and the three-dimensional structure of one rat isozyme, PLC-δ1, determined. Plants appear to contain only one gene family encoding PI-PLCs. The catalytic properties of plant PI-PLCs are very similar to those of animal enzymes. However, very little is known about the regulation of plant PI-PLCs. All plant PI-PLCs comprise three domains, X, Y and C2, which are also conserved in isoforms from animals and yeast. We here show that one PI-PLC isozyme from Arabidopsis thaliana, AtPLC2, is predominantly localized in the plasma membrane, and that the conserved N-terminal domain may represent an EF-hand domain that is required for catalytic activity but not for lipid binding.

【 授权许可】

Unknown