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

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• 作者：Otterhag ; Lotta ; Sommarin ; Marianne ; Pical ; Christophe
• 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
• 刊名：FEBS Letters
• 出版年：2001
• 出版时间：May 25, 2001
• 年：2001
• 卷：497
• 期：2-3
• 页码：165-170
• 全文大小：755 K

文摘

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.