Patatin-Related Phospholipase pPLAIII b -Induced Changes in Lipid Metabolism Alter Cellulose Content and Cell Elongation in Arabidopsis C W

Department of Biology, University of Missouri, St. Louis, Missouri 63121, USA.
The Plant Cell (Impact Factor: 9.34). 03/2011; 23(3):1107-23. DOI: 10.1105/tpc.110.081240
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The release of fatty acids from membrane lipids has been implicated in various plant processes, and the patatin-related phospholipases (pPLAs) constitute a major enzyme family that catalyzes fatty acid release. The Arabidopsis thaliana pPLA family has 10 members that are classified into three groups. Group 3 pPLAIII has four members but lacks the canonical lipase/esterase consensus catalytic sequences, and their enzymatic activity and cellular functions have not been delineated. Here, we show that pPLAIIIβ hydrolyzes phospholipids and galactolipids and additionally has acyl-CoA thioesterase activity. Alterations of pPLAIIIβ result in changes in lipid levels and composition. pPLAIIIβ-KO plants have longer leaves, petioles, hypocotyls, primary roots, and root hairs than wild-type plants, whereas pPLAIIIβ-OE plants exhibit the opposite phenotype. In addition, pPLAIIIβ-OE plants have significantly lower cellulose content and mechanical strength than wild-type plants. Root growth of pPLAIIIβ-KO plants is less sensitive to treatment with free fatty acids, the enzymatic products of pPLAIIIβ, than wild-type plants; root growth of pPLAIIIβ-OE plants is more sensitive. These data suggest that alteration of pPLAIIIβ expression and the resulting lipid changes alter cellulose content and cell elongation in Arabidopsis.

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Available from: Ruth Welti, Oct 04, 2015
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    • "RNA was converted to cDNA with RevertAid TM H Minus First Strand cDNA Synthesis kit (Fermentas, Vilnius, Lithuania). Primers were selected from previous works (Li et al. 2011; Effendi et al. 2011; see primer list). Relative expression calculation and statistical analysis were carried out with REST 2009 software (Livak & Schmittgen 2001; Pfaffl et al. 2002). "
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    ABSTRACT: pPLA-I is the evolutionarily oldest patatin-related phospholipase A (pPLA) in plants which have previously been implicated to function in auxin and defense signaling. Molecular and physiological analysis of two allelic null mutants for pPLA-I (ppla-I-1 in Wassilewskija (Ws) and ppla-I-3 in Columbia (Col) revealed pPLA-I functions in auxin and light signaling. The enzyme is localised in the cytosol and to membranes. After auxin application expression of early auxin-induced genes is significantly slower compared to wild type (WT) and both alleles show a slower gravitropic response of hypocotyls, indicating compromised auxin signaling. Additionally, phytochrome-modulated responses like abrogation of gravitropism, enhancement of phototropism and growth in far red-(FR)-enriched light are decreased in both alleles. While early flowering, root coils and delayed phototropism are only observed in the Ws mutant devoid of phyD, the light related phenotypes observed in both alleles point to an involvement of pPLA-I in phytochrome signaling. 147.
    Plant Cell and Environment 01/2014; 37(7). DOI:10.1111/pce.12278 · 6.96 Impact Factor
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    • "The localization of OssPLA2α to ER has been consistent with the earlier reports on Arabidopsis PLA2, suggesting its role in protein trafficking and pollen development [60]–[61]. Similarly, localization of PLA1 (OsPLA1-IIβ) to cytoplasm and patatin like phospholipase (OspPLA-IIIδ) to plasma membrane have been in accordance with the previous findings [13], [62] where, Arabidopsis pPLA-IIIβ protein was observed in plasma membrane and alteration in its expression modulated the cellulose content and cell elongation. The diverse sub-cellular localization of different groups of rice PLAs, suggests a significant role of OsPLAs in multiple cellular processes. "
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    ABSTRACT: Abstract BACKGROUND: Phospholipase A (PLA) is an important group of enzymes responsible for phospholipid hydrolysis in lipid signaling. PLAs have been implicated in abiotic stress signaling and developmental events in various plants species. Genome-wide analysis of PLA superfamily has been carried out in dicot plant Arabidopsis. A comprehensive genome-wide analysis of PLAs has not been presented yet in crop plant rice. METHODOLOGY/PRINCIPAL FINDINGS: A comprehensive bioinformatics analysis identified a total of 31 PLA encoding genes in the rice genome, which are divided into three classes; phospholipase A(1) (PLA(1)), patatin like phospholipases (pPLA) and low molecular weight secretory phospholipase A(2) (sPLA(2)) based on their sequences and phylogeny. A subset of 10 rice PLAs exhibited chromosomal duplication, emphasizing the role of duplication in the expansion of this gene family in rice. Microarray expression profiling revealed a number of PLA members expressing differentially and significantly under abiotic stresses and reproductive development. Comparative expression analysis with Arabidopsis PLAs revealed a high degree of functional conservation between the orthologs in two plant species, which also indicated the vital role of PLAs in stress signaling and plant development across different plant species. Moreover, sub-cellular localization of a few candidates suggests their differential localization and functional role in the lipid signaling. CONCLUSION/SIGNIFICANCE: The comprehensive analysis and expression profiling would provide a critical platform for the functional characterization of the candidate PLA genes in crop plants
    PLoS ONE 02/2012; DOI:10.1371/journal.pone.0030947 · 3.23 Impact Factor
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    ABSTRACT: This publication contains reprint articles for which IEEE does not hold copyright. Full text is not available on IEEE Xplore for these articles.
    IEEE Engineering Management Review 04/1981; DOI:10.1109/EMR.1981.4306874
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