The Arabidopsis ABHD11 Mutant Accumulates Polar Lipids in Leaves as a Consequence of Absent Acylhydrolase Activity

Vijayakumar, Anitha; Vijayaraj, Panneerselvam; Vijayakumar, Arun Kumar; Rajasekharan, Ram

doi:10.1104/pp.15.01615

Cited by 24 publications

(17 citation statements)

References 35 publications

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“…In Medicago truncatula , this gene was found to regulate the adaptation of roots to salt stress (De Lorenzo et al, ). Moreover, highly downregulated genes, such as linoleate 9S‐lipoxygenase 5 (lipoxygenase), α/β fold family protein, and phospholipase D delta, are involved in the hydrolysis of glycerol–phospholipids that are related to diverse catalytic activities of lipid (Bannenberg, Martínez, Hamberg, & Castresana, ; Vijayakumar, Vijayaraj, Vijayakumar, & Rajasekharan, ; Li et al, , respectively). Another gene for pfkb‐type carbohydrate kinase family protein was downregulated involved in the growth and development of Arabidopsis (Gilkerson, Perez‐Ruiz, Chory, & Callis, ).…”

Section: Discussionmentioning

confidence: 99%

Changes in gene expression during germination reveal pea genotypes with either “quiescence” or “escape” mechanisms of waterlogging tolerance

Zaman

Malik

Erskine

et al. 2018

Plant Cell & Environment

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Waterlogging causes germination failure in pea (Pisum sativum L.). Three genotypes (BARI Motorshuti-3, Natore local-2 [NL-2], and Kaspa) contrasting in ability to germinate in waterlogged soil were exposed to different durations of waterlogging. Whole genome RNAseq was employed to capture differentially expressing genes. The ability to germinate in waterlogged soil was associated with testa colour and testa membrane integrity as confirmed by electrical conductivity measurements. Genotypes Kaspa and NL-2 displayed different mechanisms of tolerance. In Kaspa, an energy conserving strategy was indicated by a strong upregulation of tyrosine protein kinsase and down regulation of linoleate 9S-lipoxygenase 5, a fat metabolism gene. In contrast, a faster energy utilization strategy was suggested in NL-2 by the marked upregulation of a subtilase family protein and peroxisomal adenine nucleotide carrier 2, a fat metabolizing gene. Waterlogging susceptibility in germinating seeds of genotype BARI Motorshuti-3 was linked to upregulation of a kunitz-type trypsin/protease inhibitor that blocks protein metabolism and may lead to excessive lipid metabolism and the membrane leakage associated with waterlogging damage. Pathway analyses based on gene ontologies showed seed storage protein metabolism as upregulated in tolerant genotypes and downregulated in the sensitive genotype. Understanding the tolerance mechanism provides a platform to breed for adaptation to waterlogging stress at germination in pea.

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Section: Discussionmentioning

confidence: 99%

Changes in gene expression during germination reveal pea genotypes with either “quiescence” or “escape” mechanisms of waterlogging tolerance

Zaman

Malik

Erskine

et al. 2018

Plant Cell & Environment

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“…Two encoded lipases for which little was known at the beginning of the study. PLIP1 (At3g61680) is a member of the large a,b-hydrolase gene family, of which some members play a role in lipid metabolism (Ghosh et al, 2009;James et al, 2010;Vijayakumar et al, 2016). Expression of PLIP1 is similar in dgat1-1 and wild-type seeds at 8 and 12 DAF but is more than 2-fold increased in the mutant at 16 DAF (Fig.…”

Section: Selection and Confirmation Of Genes Upregulated In Dgat1 Seedmentioning

confidence: 99%

The Plastid Lipase PLIP1 Is Critical for Seed Viability in diacylglycerol acyltransferase1 Mutant Seed

Aulakh

Durrett

2019

Plant Physiol.

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In developing Arabidopsis (Arabidopsis thaliana) seeds, the synthesis of triacylglycerol (TAG) is mediated primarily by the acyl-CoA-dependent enzyme diacylglycerol acyltransferase1 (DGAT1). In the absence of DGAT1 activity, phospholipid:diacylglycerol acyltransferase (PDAT1) plays an important role in TAG synthesis, consistent with the higherthan-expected oil content and altered fatty acid composition of dgat1 seed. Transcript profiling of developing wild type (Columbia-0) and dgat1-1 mutant seed identified 602 differentially expressed genes. Expression of genes important for the formation of phosphatidylcholine, including LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE2, and REDUCED OLEATE DESATURATION1 were strongly upregulated, consistent with increased substrate supply for PDAT1. In addition, several genes lacking a defined role in TAG biosynthesis were also upregulated, including the a/b-hydrolase family gene PLIP1, which encodes a plastid-localized lipase. In most tissues, PLIP1 was expressed at equivalent levels in wild-type and dgat1 plants, except for developing seed, where transcript levels were higher in the dgat1 mutant. Seeds from plip1 mutant plants possessed a 20% reduction in oil content and were smaller than seed from wild-type plants. Crosses between dgat1 and plip1 failed to generate double-homozygous mutant plants. Reciprocal crossing with wild-type plants demonstrated that both male and female gametophytes could transmit the dgat1 plip1 double-mutant genotype. Double-homozygous dgat1 plip1 seed formed but was green and failed to germinate. The synthetic lethal phenotype of dgat1 with plip1 indicates an important role for PLIP1 in the absence of DGAT1 activity, likely by supplying polyunsaturated fatty acid substrates for PDAT1.

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“…The phospholipase activity of Ddl1 was measured by estimating the FFA release using a fluorescent FFA estimation kit (Cayman Chemical) as reported by Vijayakumar et al (37). Nonfluorescent (native) PE and PG with different fatty acid compositions were also used for the assays.…”

Section: Expression and Purification Of The Recombinant Proteins-mentioning

confidence: 99%

Misregulation of a DDHD Domain-containing Lipase Causes Mitochondrial Dysfunction in Yeast

Yadav¹,

Rajasekharan

2016

Journal of Biological Chemistry

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The DDHD domain-containing proteins, which belong to the intracellular phospholipase A 1 (iPLA 1 ) family, have been predicted to be involved in phospholipid metabolism, lipid trafficking, membrane turnover, and signaling. Defective cardiolipin (CL), phosphatidylethanolamine, and phosphatidylglycerol remodeling cause Barth syndrome and mitochondrial dysfunction. Here, we report that Yor022c is a Ddl1 (DDHD domaincontaining lipase 1) that hydrolyzes CL, phosphatidylethanolamine, and phosphatidylglycerol. Ddl1 has been implicated in the remodeling of mitochondrial phospholipids and CL degradation. Our data also suggested that the accumulation of monolysocardiolipin is deleterious to the cells. We show that Aft1 and Aft2 transcription factors antagonistically regulate the DDL1 gene. This study reveals that the misregulation of DDL1 by Aft1/2 transcription factors alters CL metabolism and causes mitochondrial dysfunction in the cells. In humans, mutations in the DDHD1 and DDHD2 genes cause specific types of hereditary spastic paraplegia (SPG28 and SPG54, respectively), and the yeast DDL1-defective strain produces similar phenotypes of hereditary spastic paraplegia (mitochondrial dysfunction and defects in lipid metabolism). Therefore, the DDL1-defective strain could be a good model system for understanding hereditary spastic paraplegia.

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The Arabidopsis ABHD11 Mutant Accumulates Polar Lipids in Leaves as a Consequence of Absent Acylhydrolase Activity

Cited by 24 publications

References 35 publications

Changes in gene expression during germination reveal pea genotypes with either “quiescence” or “escape” mechanisms of waterlogging tolerance

Changes in gene expression during germination reveal pea genotypes with either “quiescence” or “escape” mechanisms of waterlogging tolerance

The Plastid Lipase PLIP1 Is Critical for Seed Viability in diacylglycerol acyltransferase1 Mutant Seed

Misregulation of a DDHD Domain-containing Lipase Causes Mitochondrial Dysfunction in Yeast

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