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Functional Characterization of the N-Terminal C2 Domain from Arabidopsis thaliana Phospholipase Dα and Dβ.

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Most of plant phospholipases D (PLD) exhibit a C2-lipid binding domain of around 130 amino acid residues at their N-terminal region, involved in their Ca2+-dependent membrane binding. In this study, we expressed and partially purified catalytically active PLDα from Arabidopsis thaliana (AtPLDα) in

Arabidopsis thaliana phosphoinositide-specific phospholipase C isoform 3 (AtPLC3) and AtPLC9 have an additive effect on thermotolerance.

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The heat stress response is an important adaptation, enabling plants to survive challenging environmental conditions. Our previous work demonstrated that Arabidopsis thaliana Phosphoinositide-Specific Phospholipase C Isoform 9 (AtPLC9) plays an important role in thermotolerance. During prolonged

Non-specific phospholipase C4 mediates response to aluminum toxicity in Arabidopsis thaliana.

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Aluminum ions (Al) have been recognized as a major toxic factor for crop production in acidic soils. The first indication of the Al toxicity in plants is the cessation of root growth, but the mechanism of root growth inhibition is largely unknown. Here we examined the impact of Al on the expression,

AtPLC2, a gene encoding phosphoinositide-specific phospholipase C, is constitutively expressed in vegetative and floral tissues in Arabidopsis thaliana.

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A cDNA encoding a phosphoinositide-specific phospholipase C (PI-PLC) from the higher plant Arabidopsis thaliana was cloned and characterized. The gene corresponding to this cDNA is designated AtPLC2. The overall structure of the predicted AtPLC2 protein is similar to those of plant PI-PLCs and

Phospholipase D affects translocation of NPR1 to the nucleus in Arabidopsis thaliana.

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Phytohormone salicylic acid (SA) is a crucial component of plant-induced defense against biotrophic pathogens. Although the key players of the SA pathway are known, there are still gaps in the understanding of the molecular mechanism and the regulation of particular steps. In our previous research,

The Arabidopsis thaliana genome has multiple divergent forms of phosphoinositol-specific phospholipase C1.

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Highly degenerate primers to conserved regions of the eukaryotic phosphoinositol-specific phospholipase C (PLC) were used to amplify fragments of plant PLCs from Arabidopsis thaliana genomic DNA. Eight completely different fragment sequences that showed high homology to PLCs of both animals and

Secretory phospholipase A2-alpha from Arabidopsis thaliana: functional parameters and substrate preference.

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The secretory phospholipase A2-alpha from Arabidopsis thaliana (AtsPLA2-alpha), being one of the first plant sPLA2s obtained in purified state, has been characterised with respect to substrate preference and optimum conditions of catalysis. The optima of pH, temperature, and calcium concentration

Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis thaliana.

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During a search for cDNAs encoding plant sterol acyltransferases, we isolated four full-length cDNAs from Arabidopsis thaliana that encode proteins with substantial identity with animal lecithin : cholesterol acyltransferases (LCATs). The expression of one of these cDNAs, AtLCAT3 (At3g03310), in

Secretory phospholipase A2 from Arabidopsis thaliana: insights into the three-dimensional structure and the amino acids involved in catalysis.

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A low-molecular weight phospholipase A2 from Arabidopsis thaliana, isoform phospholipase A2-alpha, has been expressed in Escherichia coli in the form of inclusion bodies, refolded, and purified to homogeneity to yield the active mature enzyme. The enzyme was characterized with respect to pH,

Evidence for and characterization of Ca2+ binding to the catalytic region of Arabidopsis thaliana phospholipase Dbeta.

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Most types of plant phospholipase D (PLD) require Ca(2+) for activity, but how Ca(2+) affects PLD activity is not well understood. We reported previously that Ca(2+) binds to the regulatory C2 domain that occurs in the N terminus of the Ca(2+)-requiring PLDs. Using Arabidopsis thaliana PLDbeta and

Phospholipase D is a negative regulator of proline biosynthesis in Arabidopsis thaliana.

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Accumulation of proline has been observed in a large number of plant species in response to drought and salt stresses, suggesting a key role of this amino acid in plant stress adaptation. Upstream components of the proline biosynthesis signal transduction pathways are still poorly defined. We

Probing selected structural regions in the secreted phospholipase A₂ from Arabidopsis thaliana for their impact on stability and activity.

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In contrast to the well characterized secreted phospholipases A2 (sPLA2) from animals, their homologues from plants have been less explored. Their production in purified form is more difficult, and no data on their stability are known. In the present paper, different variants of the sPLA2 isoform α

Expression of the patatin-related phospholipase A gene AtPLA IIA in Arabidopsis thaliana is up-regulated by salicylic acid, wounding, ethylene, and iron and phosphate deficiency.

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In Arabidopsis thaliana (L.) Heynh., the cytosolic, patatin-related phospholipase A enzymes comprise a family of ten genes designated AtPLAs thought to be involved in auxin and pathogen signalling [A. Holk et al. (2002) Plant Physiol 130:90-101]. One of these, AtPLA IIA, is investigated here by

[Phospholipase Dα1 and hydrogen sulfide were involved in the allelopathy of oridonin to Arabidopsis thaliana]

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We investigated the signal relationship between phospholipase Dα1 (PLDα1) and the gas signal molecule hydrogen sulfide (H₂S) in Arabidopsis thaliana response to the allelopathy of diterpenoid oridonin. The wild type Arabidopsis Columbia (WT), phospholipase Dα1 (PLDα1) deletion mutant

N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana.

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Phosphoinositide-specific phospholipase C's (PI-PLCs) are ubiquitous in eukaryotes, from plants to animals, and catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate into the two second messengers inositol 1,4,5-trisphosphate and diacylglycerol. In animals, four distinct subfamilies of

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