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JXB Advance Access published online on April 8, 2004
Journal of Experimental Botany, doi:10.1093/jxb/erh140
© 2004 by Oxford University Press
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Received December 3, 2003; accepted February 26, 2004
© 2004 Society for Experimental Biology

GENE NOTE

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

Koji Mikami 1*, Alexander Repp 2, Elena Graebe-Abts 2, and Elmar Hartmann 2

1 National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki 444-8585, Japan
2 Institut für Biologie-Pflanzenphysiologie, Freie Universität Berlin, Königin-Luise-Str. 12-16, D-14195 Berlin, Germany

* To whom correspondence should be addressed. E-mail: mikami{at}nibb.ac.jp.


  Abstract

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.

Key words: Phosphoinositide-specific phospholipase C, Physcomitrella patens, substrate preference.


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