Glutathione Transferases

Dixon, David P.; Edwards, Robert

doi:10.1199/tab.0131

Cited by 198 publications

(229 citation statements)

References 87 publications

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“…Previous research revealed that overexpression of members of the Arabidopsis GST superfamily in Escherichia coli resulted in 25 of the 28 GST tau (U) proteins (GSTUs) causing an aberrant accumulation of acylated GSH thioesters in vivo, a perturbation that was not observed with other GST classes (47). In particular, the study demonstrated that GSTU members catalyzed the S-glutathionylation of 12-oxo-phytodienoic acid (OPDA), an early biosynthetic precursor of JA (28,47). Further research is required to determine whether FIP1 plays a role in other regulatory mechanisms in jasmonic acid signaling, such as preventing epimerization of the active (+)-7-iso-jasmonoyl-L-isoleucine attaching to the inactive (−)-jasmonoyl-L-isoleucine.…”

Section: The Conserved Residues Compose Three Motifs: Motif I (S/t-mentioning

confidence: 86%

“…The kinetic assay for GST activity of FIP1 was analyzed by the CDNB assay to determine the production of GS-DNB (28). Protein samples were incubated with 100 mM NaH 2 PO 4 (pH 6.5), 1 mM GSH, and various concentrations of CDNB (0.1-3 mM) at 25°C for 5 min.…”

Section: Methodsmentioning

confidence: 99%

“…This family is involved in diverse functions, including detoxification and reduction of oxidative stress (27)(28)(29). FIP1 has a GST activity of specific affinity to glutathione (GSH) and 1-chloro-2,4-dinitrobenzene Significance Far-red (FR) insensitive 219 (FIN219) is the main jasmonate (JA)-amido synthetase that activates the systemic synthesis of bioactive JAs in Arabidopsis.…”

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confidence: 99%

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Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation

Chen

Kuo

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Far-red (FR) light-coupled jasmonate (JA) signaling is necessary for plant defense and development. FR insensitive 219 (FIN219) is a member of the Gretchen Hagen 3 (GH3) family of proteins in Arabidopsis and belongs to the adenylate-forming family of enzymes. It directly controls biosynthesis of jasmonoyl-isoleucine in JA-mediated defense responses and interacts with FIN219-interacting protein 1 (FIP1) under FR light conditions. FIN219 and FIP1 are involved in FR light signaling and are regulators of the interplay between light and JA signaling. However, how their interactions affect plant physiological functions remains unclear. Here, we demonstrate the crystal structures of FIN219-FIP1 while binding with substrates at atomic resolution. Our results show an unexpected FIN219 conformation and demonstrate various differences between this protein and other members of the GH3 family. We show that the rotated C-terminal domain of FIN219 alters ATP binding and the core structure of the active site. We further demonstrate that this unique FIN219-FIP1 structure is crucial for increasing FIN219 activity and determines the priority of substrate binding. We suggest that the increased FIN219 activity resulting from the complex form, a conformation for domain switching, allows FIN219 to switch to its high-affinity mode and thereby enhances JA signaling under continuous FR light conditions. jasmonate response | far-red light | signaling cross-talk | adenylation enzyme | phytohormone F ar-red (FR) insensitive 219 (FIN219) (1), also known as jasmonate (JA) resistant 1 (JAR1; AtGH3.11) (2), is a member of the auxin-regulated Gretchen Hagen 3 (GH3) family of proteins (3). The GH3 family in Arabidopsis is composed of 19 distinct proteins and is also conserved in plants such as rice (4-6), tomato (7,8), and maize (9), with 13, 15, and 13 members, respectively. Phylogenetically, the GH3 family is classified as part of the adenylate-forming enzyme superfamily, which contains proteins such as firefly luciferase-like enzymes (10). This diverse group of enzymes catalyzes the addition of AMP to carboxyl groups on a wide variety of substrates and typically contains three conserved motifs that form a binding pocket for ATP and AMP substrate intermediates (11). GH3 proteins regulate the activity of plant hormones through amino acid conjugation and have a substantial effect on plant metabolism and physiology (12). For example, FIN219 catalyzes the conjugation of isoleucine (Ile) to JA, forming jasmonoyl-isoleucine (JA-Ile). This reaction results in the degradation of the transcriptional repressor JA-ZIM (zinc-finger protein expressed in inflorescence meristem) domain (JAZ) proteins and the subsequent activation of downstream transcriptional responses (13).FIN219 has been identified in suppressor screenings using a temperature sensitive constitutive photomorphogenic 1 (cop1) mutant line. It is involved in FR light-mediated inhibition of hypocotyl elongation and regulates light inactivation of COP1 activity (1). Furthermore, FIN219 acts as a ...

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Section: The Conserved Residues Compose Three Motifs: Motif I (S/t-mentioning

confidence: 86%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation

Chen

Kuo

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…The GSTs in plants have antioxidant properties that can scavenge ROS and other toxic compounds, maintain redox homeostasis, and mediate biosynthesis of certain defense molecules; however, specific function vary by the class [66][67][68]. Our study identified altered expression of seven transcripts putatively associated with GSTs in response to greenbug infestation (Fig.…”

Section: Gsts Peroxidases and Redox State Related Transcriptsmentioning

confidence: 99%

“…GSTF2 related transcripts localized in the plasma membrane encoding phi class of plant-specific proteins mediating phytohormone induced oxidative stress [67,68]. The only GST transcript upregulated in RB (ta.1878.3.s1_at) was putatively associated with membrane associated proteins in eicosanoid and glutathione metabolism (MAPEG-like protein) and is also involved in detoxification functions [69].…”

Section: Gsts Peroxidases and Redox State Related Transcriptsmentioning

confidence: 99%

Transcriptomics of induced defense responses to greenbug aphid feeding in near isogenic wheat lines

et al. 2013

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Structural evidence for Arabidopsis glutathione transferase AtGSTF2 functioning as a transporter of small organic ligands

et al. 2016

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Glutathione transferases (GSTs) are involved in many processes in plant biochemistry, with their best characterised role being the detoxification of xenobiotics through their conjugation with glutathione. GSTs have also been implicated in noncatalytic roles, including the binding and transport of small heterocyclic ligands such as indole hormones, phytoalexins and flavonoids. Although evidence for ligand binding and transport has been obtained using gene deletions and ligand binding studies on purified GSTs, there has been no structural evidence for the binding of relevant ligands in noncatalytic sites. Here we provide evidence of noncatalytic ligand‐binding sites in the phi class GST from the model plant Arabidopsis thaliana , At GSTF2, revealed by X‐ray crystallography. Complexes of the At GSTF2 dimer were obtained with indole‐3‐aldehyde, camalexin, the flavonoid quercetrin and its non‐rhamnosylated analogue quercetin, at resolutions of 2.00, 2.77, 2.25 and 2.38 Å respectively. Two symmetry‐equivalent‐binding sites ( L1 ) were identified at the periphery of the dimer, and one more ( L2 ) at the dimer interface. In the complexes, indole‐3‐aldehyde and quercetrin were found at both L1 and L2 sites, but camalexin was found only at the L1 sites and quercetin only at the L2 site. Ligand binding at each site appeared to be largely determined through hydrophobic interactions. The crystallographic studies support previous conclusions made on ligand binding in noncatalytic sites by At GSTF2 based on isothermal calorimetry experiments (Dixon et al . (2011) Biochem J 438 , 63–70) and suggest a mode of ligand binding in GSTs commensurate with a possible role in ligand transport.

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Glutathione Transferases

Cited by 198 publications

References 87 publications

Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation

Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation

Transcriptomics of induced defense responses to greenbug aphid feeding in near isogenic wheat lines

Structural evidence for Arabidopsis glutathione transferase AtGSTF2 functioning as a transporter of small organic ligands

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