NDLI: Molecular Identification of Cytosolic, Patatin-Related Phospholipases A from Arabidopsis with Potential Functions in Plant Signal Transduction1

Content Provider	PubMed Central
Author	Holk, André Rietz, Steffen Zahn, Marc Quader, Hartmut Scherer, Günther F. E.
Copyright Year	2002
Abstract	Rapid activation of phospholipase A (PLA) by auxin or plant-pathogen interaction suggests a function in signal transduction for this enzyme, but the molecular identification of a cytosolic PLA carrying out this function remains open. We isolated four cDNA sequences from Arabidopsis (ecotype Columbia), AtPLA I, AtPLA IIA, AtPLA IVA, and AtPLA IVC, which are members of the patatin-related PLA gene family in plants and which are homologous to the animal Ca2+-independent PLA2 gene family. Expression was measured by reverse transcriptase-polymerase chain reaction, and AtPLA I transcripts were found preferentially in shoots, AtPLA IIA and AtPLA IVA in roots, and AtPLA IVC in flowers. Transient expression of the four PLA-green fluorescent protein fusion proteins in tobacco (Nicotiana tabacum) leaves showed they were located in the cytosol and not in the vacuoles. Surprisingly, AtPLA::green fluorescent protein was also localized to chloroplasts. The enzymatic activity of the purified recombinant AtPLA IVA toward phosphatidylcholine was dependent on Ca2+, saturated at 0.5 mm, and had a pH optimum of about 7.0. It had both PLA1 and PLA2 specificity. The enzyme showed in vitro highest sensitivity toward the PLA2 inhibitors palmitoyltrifluoromethyl ketone (PACOCF3, K i approximately 30 nm), arachidonyltrifluoromethyl ketone (AACOCF3, K i approximately 25 μm), and tetrahydro-3-(1-naphtalenyl)-2H-pyran-2-one (K i approximately 200 nm) and was also sensitive to other previously used inhibitors 5,8,11,14-eicosatetraynoic acid (K i approximately 3 μm) and nordihydroguajaretic acid (K i approximately 15 μm). The influence of these PLA2 inhibitors on elongation in etiolated Arabidopsis seedlings was tested, and tetrahydro-3-(1-naphtalenyl)-2H-pyran-2-one and 5,8,11,14-eicosatetraynoic acid inhibited hypocotyl elongation maximally at concentrations close to their K i in vitro.
Related Links	http://dx.doi.org/10.1104/pp.006288
Ending Page	101
Page Count	12
Starting Page	90
File Format	PDF
ISSN	00320889
e-ISSN	15322548
Journal	Plant Physiology
Issue Number	1
Volume Number	130
Language	English
Publisher	American Society of Plant Physiologists
Publisher Date	2002-09-01
Access Restriction	Open
Rights Holder	American Society of Plant Physiologists
Subject Keyword	Plant Science Genetics Physiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Physiology Plant Science

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