Abstract
Lipid acyl hydrolase are a diverse group of enzymes that hydrolyze the ester or amide bonds of fatty acid in plant lipids. Patatin-related phospholipase AIIIs (pPLAIIIs) are one of major lipid acyl hydrolases that are less closely related to potato tuber patatins and are plant-specific. Recently, overexpression of ginseng-derived PgpPLAIIIβ was reported to be involved in the reduced level of lignin content in Arabidopsis and the mature xylem layer of poplar. The presence of lignin-polysaccharides renders cell walls recalcitrant for pulping and biofuel production. The tissue-specific regulation of lignin biosynthesis, without altering all xylem in plants, can be utilized usefully by keeping mechanical strength and resistance to various environmental stimuli. To identify another pPLAIII homolog from Arabidopsis, constitutively overexpressed AtpPLAIIIα was characterized for xylem lignification in two well-studied model plants, Arabidopsis and poplar. The characterization of gene function in annual and perennial plants with respect to lignin biosynthesis revealed the functional redundancy of less lignification via downregulation of lignin biosynthesis-related genes.
Highlights
Plant phospholipase A (PLA) families are classified into two groups: low-molecular-weight PLA2 s and patatin-related PLAs, which hydrolyze an acyl ester bond of glycerolipids to liberate free fatty acids and lysophospholipids [1,2]
Constitutive overexpression lines of AtpPLAIIIα under the 35S cauliflower mosaic virus promoter with an mRFP-tagged end of C-terminal region were generated by Agrobacterium-mediated floral dipping method [12]
Endogenous displayed a reduced amount of lignin instead of cellulose content alteration (Figure 2), which is AtpPLAIIIα-OE displayed a reduced amount of lignin instead of cellulose content alteration antagonistic to that found in rice focused on cell wall composition [7]
Summary
Plant phospholipase A (PLA) families are classified into two groups: low-molecular-weight PLA2 s and patatin-related PLAs (pPLAs), which hydrolyze an acyl ester bond of glycerolipids to liberate free fatty acids and lysophospholipids [1,2]. The molecular and biochemical functions of patatin-related phospholipases such as AtpPLAIIIβ and AtpPLAIIIδ were characterized and were found to cause short and stunted phenotypic characteristics with increasing phospholipids and galactolipids in Arabidopsis [5,6,10]. The altered lipid species were reported to result in the reduction of cellulose content [5,6] Another close homolog AtpPLAIIIα was only functionally characterized in rice and showed a similar phenotype to AtpPLAIIIβ-OE and AtpPLAIIIδ-OE, but the contents of many lipid species were lower than that of wild-type (WT)
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