| Literature DB >> 15073208 |
Koji Mikami1, Alexander Repp, Elena Graebe-Abts, Elmar Hartmann.
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.Entities:
Mesh:
Substances:
Year: 2004 PMID: 15073208 DOI: 10.1093/jxb/erh140
Source DB: PubMed Journal: J Exp Bot ISSN: 0022-0957 Impact factor: 6.992