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The Arabidopsis Phospholipase D Family. Characterization of a Calcium-Independent and Phosphatidylcholine-Selective PLDζ1 with Distinct Regulatory Domains

The Arabidopsis Phospholipase D Family. Characterization of a Calcium-Independent and Phosphatidylcholine-Selective PLDζ1 with Distinct Regulatory Domains Four types of phospholipase D (PLD), PLDα, β, γ, and δ, have been characterized in Arabidopsis, and they display different requirements for Ca 2+ , phosphatidylinositol 4,5-bisphosphate (PIP 2 ), substrate vesicle composition, and/or free fatty acids. However, all previously cloned plant PLDs contain a Ca 2+ -dependent phospholipid-binding C2 domain and require Ca 2+ for activity. This study documents a new type of PLD, PLDζ1, which is distinctively different from previously characterized PLDs. It contains at the N terminus a Phox homology domain and a pleckstrin homology domain, but not the C2 domain. A full-length cDNA for Arabidopsis PLDζ1 has been identified and used to express catalytically active PLD in Escherichia coli . PLDζ1 does not require Ca 2+ or any other divalent cation for activity. In addition, it selectively hydrolyzes phosphatidylcholine, whereas the other Arabidopsis PLDs use several phospholipids as substrates. PLDζ1 requires PIP 2 for activity, but unlike the PIP 2 -requiring PLDβ or γ, phosphatidylethanolamine is not needed in substrate vesicles. These differences are described, together with a genomic analysis of 12 putative Arabidopsis PLD genes that are grouped into α, β, δ, γ, and ζ based on their gene architectures, sequence similarities, domain structures, and biochemical properties. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Physiology American Society of Plant Biologist

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