Adducts of Oxylipin Electrophiles to Glutathione Reflect a 13 Specificity of the Downstream Lipoxygenase Pathway in the Tobacco Hypersensitive Response

Davoine, Céline; Falletti, Olivier; Douki, Thierry; Iacazio, Gilles; Ennar, Najla; Montillet, Jean‐Luc; Triantaphylidès, C.

doi:10.1104/pp.105.074690

Cited by 82 publications

(84 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…3). Such GSH conjugates accumulate in plants fed with oxylipins or exposed to infection (30,31). Although it is possible that GSTUs bind these conjugates after their spontaneous glutathionylation, our studies demonstrated that GSTU19 and other GSTUs actively catalyzed the formation of the OPDA conjugate.…”

Section: Discussionmentioning

confidence: 82%

“…The physiological consequence of oxylipin conjugation in plants is unknown, although similar derivatives of the chemically related leukotrienes are known to be bioactive in mammals (32). It is also of interest that OPDA is an intermediate in jasmonic acid synthesis and that GSTU19 may have a role in regulating the passage of this compound from the chloroplast to the peroxisome (31).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Selective Binding of Glutathione Conjugates of Fatty Acid Derivatives by Plant Glutathione Transferases

Dixon

Edwards

2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

Proteomic studies with Arabidopsis thaliana have revealed that the plant-specific Tau (U) class glutathione transferases (GSTs) are selectively retained by S-hexylglutathione affinity supports. Overexpression of members of the Arabidopsis GST superfamily in Escherichia coli showed that 25 of the complement of 28 GSTUs caused the aberrant accumulation of acylated glutathione thioesters in vivo, a perturbation that was not observed with other GST classes. Each GSTU caused a specific group of fatty acyl derivatives to accumulate, which varied in chain length (C 6 to C 18 ), additional oxygen content (0 or 1), and desaturation (0 or 1). Thioesters bound tightly to recombinant GSTs (K d ϳ 1 M), explaining their accumulation. Transient expression of GSTUs in Nicotiana benthamiana followed by recovery by Strep-tag affinity chromatography allowed the respective plant ligands to be extracted and characterized. Again, each GST showed a distinct profile of recovered metabolites, notably glutathionylated oxophytodienoic acid and related oxygenated fatty acids. Similarly, the expression of the major Tau protein GSTU19 in the endogenous host Arabidopsis led to the selective binding of the glutathionylated oxophytodienoic acid-glutathione conjugate, with the enzyme able to catalyze the conjugation reaction. Additional ligands identified in planta included other fatty acid derivatives including divinyl ethers and glutathionylated chlorogenic acid. The strong and specific retention of various oxygenated fatty acids by each GSTU and the conservation in binding observed in the different hosts suggest that these proteins have selective roles in binding and conjugating these unstable metabolites in vivo.In plants, the glutathione transferases (GSTs 2 ; EC 2.5.1.18) are a superfamily of proteins with the dominant Phi (F) and Tau (U) classes having largely undefined functions in endogenous metabolism (1). This is in contrast to their relatively well studied role in catalyzing the glutathione conjugation of herbicides (2). Because of their importance in determining herbicide selectivity, these proteins have been purified from a range of major crops including maize (3), soybean (4), and wheat (5, 6). One approach which has been commonly applied to isolate these proteins is affinity chromatography using a range of glutathione (GSH) derivatives as ligands (7). These ligands often display a surprising degree of selectivity in capturing specific GSTs. Thus, in wheat extracts, whereas GSH-agarose effectively isolated GSTFs, S-hexylglutathione (GS-hexyl) proved to be a selective ligand for GSTUs (5). Similarly, glutathionylated dyes have proved to be highly selective for specific GSTs in maize (8).In each application, the use of GSH derivatives as affinity ligands has been developed through serendipity, with limited attention directed to the potential significance of such binding selectivity in relating to the nature of in vivo substrates and reaction products. At a molecular level, crystallographic studies with both plant GSTFs (9) and GSTUs...

show abstract

Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Selective Binding of Glutathione Conjugates of Fatty Acid Derivatives by Plant Glutathione Transferases

Dixon

Edwards

2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…This acetylation has been hypothesized to play a role in the inactivation and turnover of C6-aldehydes (d 'Auria et al, 2006;Farag et al, 2005). Secondly, in addition to acetylation, exogenously applied E-2-hexenal can also undergo conjugation to glutathione (GSH), leading to the formation of E-2-hexenal GSH adducts in the form of 1-hexanol-3-GSH (Davoine et al, 2006). Conjugation to GSH is a well-known mechanism to inactivate reactive molecules (Coleman et al, 1997).…”

Section: Gaba Stimulates Root Growth Of E-2-hexenal-treated Her1 Seedmentioning

confidence: 99%

“…The solution was centrifuged at 8000 g for 5 min and, subsequently, the supernatant was filtered and used for the electrospray ionization HPLC-MS 2 analysis according to the method described by Davoine et al (2005). Quantification was carried out in the MRM mode, following the specific mass transition 408 fi 279 corresponding to the loss of glutamyl (129) from the ion (1-hexanol -3-GSH + H + ) as described by Davoine et al (2006).…”

Section: Determination Of Gsh Adduct Levelsmentioning

confidence: 99%

See 1 more Smart Citation

The Arabidopsis her1 mutant implicates GABA in E‐2‐hexenal responsiveness

Mirabella¹,

Rauwerda

Struys

et al. 2007

The Plant Journal

View full text Add to dashboard Cite

SummaryWhen wounded or attacked by herbivores or pathogens, plants produce a blend of six-carbon alcohols, aldehydes and esters, known as C6-volatiles. Undamaged plants, when exposed to C6-volatiles, respond by inducing defense-related genes and secondary metabolites, suggesting that C6-volatiles can act as signaling molecules regulating plant defense responses. However, to date, the molecular mechanisms by which plants perceive and respond to these volatiles are unknown. To elucidate such mechanisms, we decided to isolate Arabidopsis thaliana mutants in which responses to C6-volatiles were altered. We observed that treatment of Arabidopsis seedlings with the C6-volatile E-2-hexenal inhibits root elongation. Among C6-volatiles this response is specific to E-2-hexenal, and is not dependent on ethylene, jasmonic and salicylic acid. Using this bioassay, we isolated 18 E-2-hexenal-response (her) mutants that showed sustained root growth after E-2-hexenal treatment. Here, we focused on the molecular characterization of one of these mutants, her1. Microarray and map-based cloning revealed that her1 encodes a c-amino butyric acid transaminase (GABA-TP), an enzyme that degrades GABA. As a consequence of the mutation, her1 plants accumulate high GABA levels in all their organs. Based on the observation that E-2-hexenal treatment induces GABA accumulation, and that high GABA levels confer resistance to E-2-hexenal, we propose a role for GABA in mediating E-2-hexenal responses.

show abstract

The Rise and Fall of Jasmonate Biological Activities

Heitz

Smirnova

Widemann

et al. 2016

Subcellular Biochemistry

View full text Add to dashboard Cite

Jasmonates (JAs) constitute a major class of plant regulators that coordinate responses to biotic and abiotic threats and important aspects of plant development. The core biosynthetic pathway converts linolenic acid released from plastid membrane lipids to the cyclopentenone cis-oxo-phytodienoic acid (OPDA) that is further reduced and shortened to jasmonic acid (JA) in peroxisomes. Abundant pools of OPDA esterified to plastid lipids also occur upon stress, mainly in the Arabidopsis genus. Long thought to be the bioactive hormone, JA only gains its pleiotropic hormonal properties upon conjugation into jasmonoyl-isoleucine (JA-Ile). The signaling pathway triggered when JA-Ile promotes the assembly of COI1-JAZ (Coronatine Insensitive 1-JAsmonate Zim domain) co-receptor complexes has been the focus of most recent research in the jasmonate field. In parallel, OPDA and several other JA derivatives are recognized for their separate activities and contribute to the diversity of jasmonate action in plant physiology. We summarize in this chapter the properties of different bioactive JAs and review elements known for their perception and signal transduction. Much progress has also been gained on the enzymatic processes governing JA-Ile removal. Two JA-Ile catabolic pathways, operating through ω-oxidation (cytochromes P450) or conjugate cleavage (amido hydrolases) shape signal dynamics to allow optimal control on defense. JA-Ile turnover not only participates in signal attenuation, but also impact the homeostasis of the entire JA metabolic pathway.

show abstract

Adducts of Oxylipin Electrophiles to Glutathione Reflect a 13 Specificity of the Downstream Lipoxygenase Pathway in the Tobacco Hypersensitive Response

Cited by 82 publications

References 52 publications

Selective Binding of Glutathione Conjugates of Fatty Acid Derivatives by Plant Glutathione Transferases

Selective Binding of Glutathione Conjugates of Fatty Acid Derivatives by Plant Glutathione Transferases

The Arabidopsis her1 mutant implicates GABA in E‐2‐hexenal responsiveness

The Rise and Fall of Jasmonate Biological Activities

Contact Info

Product

Resources

About