Isolation of cDNAs encoding typical and novel types of phosphoinositide-specific phospholipase C from the moss Physcomitrella patens

Two cDNAs encoding proteins, PpPLC1 and PpPLC2, with catalytic and C2 domains conserved in plant phosphoinositide-specific phospholipase C (PI-PLC) were isolated from Physcomitrella patens. The N domain, which has been identified in Arabidopsis PI-PLCs as an EF hand-like domain, was found in both is...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 55(2004), 401 vom: 25. Juni, Seite 1437-9
1. Verfasser: Mikami, Koji (VerfasserIn)
Weitere Verfasser: Repp, Alexander, Graebe-Abts, Elena, Hartmann, Elmar
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't DNA, Complementary Plant Proteins Phosphoinositide Phospholipase C EC 3.1.4.11 Phosphatidylinositol Diacylglycerol-Lyase EC 4.6.1.13
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245 1 0 |a Isolation of cDNAs encoding typical and novel types of phosphoinositide-specific phospholipase C from the moss Physcomitrella patens 
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520 |a Two cDNAs encoding proteins, PpPLC1 and PpPLC2, with catalytic and C2 domains conserved in plant phosphoinositide-specific phospholipase C (PI-PLC) were isolated from Physcomitrella patens. The N domain, which has been identified in Arabidopsis PI-PLCs as an EF hand-like domain, was found in both isoforms, although that in PpPLC2 was a split type. At micromolar Ca2+ concentrations, PpPLC1 preferentially hydrolysed phosphatidylinositol-4,5-bisphosphate, while PpPLC2 showed no specificity. Furthermore, at millimolar Ca2+, phosphatidylinositol was hydrolysed by PpPLC2, but not by PpPLC1. Thus, PpPLC1 and PpPLC2 are typical and novel types of plant PI-PLC, respectively 
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700 1 |a Graebe-Abts, Elena  |e verfasserin  |4 aut 
700 1 |a Hartmann, Elmar  |e verfasserin  |4 aut 
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