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First published online February 24, 2002; 10.1104/pp.010928

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Plant Physiol, March 2002, Vol. 128, pp. 1057-1068

The Arabidopsis Phospholipase D Family. Characterization of a Calcium-Independent and Phosphatidylcholine-Selective PLDzeta 1 with Distinct Regulatory Domains1

Chunbo Qin and Xuemin Wang*

Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506

Four types of phospholipase D (PLD), PLDalpha , beta , gamma , and delta , have been characterized in Arabidopsis, and they display different requirements for Ca2+, phosphatidylinositol 4,5-bisphosphate (PIP2), substrate vesicle composition, and/or free fatty acids. However, all previously cloned plant PLDs contain a Ca2+-dependent phospholipid-binding C2 domain and require Ca2+ for activity. This study documents a new type of PLD, PLDzeta 1, 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 PLDzeta 1 has been identified and used to express catalytically active PLD in Escherichia coli. PLDzeta 1 does not require Ca2+ or any other divalent cation for activity. In addition, it selectively hydrolyzes phosphatidylcholine, whereas the other Arabidopsis PLDs use several phospholipids as substrates. PLDzeta 1 requires PIP2 for activity, but unlike the PIP2-requiring PLDbeta or gamma , 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 alpha , beta , delta , gamma , and zeta  based on their gene architectures, sequence similarities, domain structures, and biochemical properties.

1 This work was supported by the National Science Foundation (grant no. IBN-9808729) and the U.S. Department of Agriculture (2001-35304-10087). This is contribution 02-142-J of the Kansas Agricultural Experiment Station.

* Corresponding author; e-mail wangs{at}ksu.edu; fax 785-532-7278.

© 2002 American Society of Plant Physiologists


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