Disease relevance of AT4G20670

• Crystal structure of a thermostable lipase from Bacillus stearothermophilus P1 [1].
• Recombinant lipase protein produced in Escherichia coli preferentially hydrolyzed phospholipids, indicating that the gene encodes a phospholipase [2].
• An Arabidopsis cDNA called AtLip1 (At2g15230), which exhibits strong homology to lysosomal acid lipase, was found to drive the synthesis of an active TAG lipase when expressed in the baculovirus system [3].

High impact information on AT4G20670

• The Arabidopsis EDS1 and PAD4 genes encode lipase-like proteins that function in resistance (R) gene-mediated and basal plant disease resistance [4].
• The recombinant GLIP1 protein possessed lipase and antimicrobial activities that directly disrupt fungal spore integrity [5].
• We identified the DAD1 gene by T-DNA tagging, which is characteristic to a putative N-terminal transit peptide and a conserved motif found in lipase active sites [6].
• Induction by both elicitors is not dependent on salicylic acid or EDS1, a putative lipase involved in defense signaling [7].
• Cloning of chlorophyllase, the key enzyme in chlorophyll degradation: finding of a lipase motif and the induction by methyl jasmonate [8].

Biological context of AT4G20670

• The deduced amino acid sequence (347 aa residues) had a lipase motif overlapping with an ATP/GTP-binding motif (P-loop) [8].
• An Arabidopsis expressed sequence tag clone, 221D24, encoding a lipase has been characterized using an antisense approach [2].
• The lipase gene is expressed during normal growth and development of Arabidopsis rosette leaves but is down-regulated as the leaves senesce [2].
• The open reading frame (ORF) of 1278 nucleotides coded for a predicted 426-amino-acid protein (CnLyso1p) with two highly conserved GXSXG lipase-specific catalytic motifs and a molecular weight of 48.3 kDa [9].
• Lipase catalysed 1,3-specific lipolysis of triacylglycerol from transformed plants demonstrated that ricinoleic acid is not excluded from the sn-2 position of triacylglycerol, but is the only hydroxy fatty acid present at this position [10].

Anatomical context of AT4G20670

• Biosynthesis of 12-oxophytodienoic acid from alpha-linolenic acid occurs in plastids, mainly in chloroplasts, and is thought to start with free linolenic acid liberated from membrane lipids by lipase action [11].
• In plasma membranes from oat, however, a phospholipase D-type activity and a phosphatidic acid phosphatase were the dominant lipase activities induced by phosphate deficiency [12].
• The lipase protein is localized in the cell cytosol and is present in all organs of Arabidopsis plants [2].

Associations of AT4G20670 with chemical compounds

• In a differential screening between Arabidopsis plants pretreated with the resistance-inducer beta-aminobutyric acid and untreated control plants, we have identified a gene encoding a novel lipase-like protein, PRLIP1 [13].
• The aim of this study was to design a convenient, specific, sensitive, and continuous lipase activity assay using natural long-chain triacylglycerols (TAGs) [14].
• The lipase had a maximal activity at pH 6 and the specific activity was estimated to be about 45 micromol min(-1) mg(-1) protein using triolein as a substrate [3].
• Moreover, this lipase showed the highest specificity for the studied reaction, i.e., high selectivity for the reaction with triricinolein but low for 1,2(2,3)-diricinolein [15].
• Collectively, it is suggested that the lipolytic enzyme involved in the short-chain aldehyde formation is a galactolipid-specific lipase [16].

Other interactions of AT4G20670

• We have isolated a novel halotolerance gene from Arabidopsis thaliana, A. thaliana Li-tolerant lipase 1 (AtLTL1), on the basis of the phenotype of tolerance to LiCl conferred by its expression in yeast [17].
• The similarity between MyAP and a lipase from Arabidopsis thaliana indicated a possible function in liberating acylated glucosinolates from their acyl group, thereby making them available for hydrolysis by the myrosinase enzymes [18].
• Transgenic Arabidopsis plants in which levels of the senescence-induced lipase protein have been reduced show delayed leaf senescence [19].

References