Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids

Sylvestre-Gonon, Elodie; Morette, Laura; Viloria, Morgane; Mathiot, Sandrine; Boutilliat, Alexis; Favier, F.; Rouhier, Nicolas; Didierjean, Claude; Hecker, Arnaud

doi:10.3389/fmolb.2022.958586

Cited by 4 publications

(1 citation statement)

References 67 publications

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“…This showed that the site where the zwitterionic fragment of GSH was located was an electrophilic site. This property is verified in the crystallographic structures of glutathione-free GSTs because they often contain a negative ion in this site such as chloride, acetate or formate ions [ 56 ]. In addition, this electrophilic site was found to be catalytically important as it hosts the γ-Glu carboxylate group which is presumed to decrease the pKa of the GSH thiol group [ 57 ].…”

Section: Resultsmentioning

confidence: 98%

Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803

et al. 2022

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Glutathione transferases (GSTs) constitute a widespread superfamily of enzymes notably involved in detoxification processes and/or in specialized metabolism. In the cyanobacterium Synechocsytis sp. PCC 6803, SynGSTC1, a chi-class GST (GSTC), is thought to participate in the detoxification process of methylglyoxal, a toxic by-product of cellular metabolism. A comparative genomic analysis showed that GSTCs were present in all orders of cyanobacteria with the exception of the basal order Gloeobacterales. These enzymes were also detected in some marine and freshwater noncyanobacterial bacteria, probably as a result of horizontal gene transfer events. GSTCs were shorter of about 30 residues compared to most cytosolic GSTs and had a well-conserved SRAS motif in the active site (10SRAS13 in SynGSTC1). The crystal structure of SynGSTC1 in complex with glutathione adopted the canonical GST fold with a very open active site because the α4 and α5 helices were exceptionally short. A transferred multipolar electron-density analysis allowed a fine description of the solved structure. Unexpectedly, Ser10 did not have an electrostatic influence on glutathione as usually observed in serinyl-GSTs. The S10A variant was only slightly less efficient than the wild-type and molecular dynamics simulations suggested that S10 was a stabilizer of the protein backbone rather than an anchor site for glutathione.

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Section: Resultsmentioning

confidence: 98%

Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803

et al. 2022

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Genome-wide identification of poplar GSTU gene family and its PtrGSTU23 and PtrGSTU40 to improve salt tolerance in poplar

Niu,

Feng,

Liu

et al. 2024

Industrial Crops and Products

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Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?

Micic,

Holmelund Rønager,

Sørensen

et al. 2024

Phil. Trans. R. Soc. B

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Plant glutathione transferases (GSTs) constitute a large and diverse family of enzymes that are involved in plant stress response, metabolism and defence, yet their physiological functions remain largely elusive. Consistent with the traditional view on GSTs across organisms as detoxification enzymes, in vitro most plant GSTs catalyse glutathionylation, conjugation of the tripeptide glutathione (GSH; γ-Glu-Cys-Gly) onto reactive molecules. However, when it comes to elucidating GST functions, it remains a key challenge that the endogenous plant glutathione conjugates (GS-conjugates) that would result from such glutathionylation reactions are rarely reported. Furthermore, GSTs often display high substrate promiscuity, and their proposed substrates are prone to spontaneous chemical reactions with GSH; hence, single-gene knockouts rarely provide clear chemotypes or phenotypes. In a few cases, GS-conjugates are demonstrated to be biosynthetic intermediates that are rapidly further metabolized towards a pathway end product, explaining their low abundance and rare detection. In this review, we summarize the current knowledge of plant GST functions and how and possibly why evolution has resulted in a broad and extensive expansion of the plant GST family. Finally, we demonstrate that endogenous GS-conjugates are more prevalent in plants than assumed and suggest they are overlooked as clues towards the identification of plant GST functions. This article is part of the theme issue ‘The evolution of plant metabolism’.

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Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids

Cited by 4 publications

References 67 publications

Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803

Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803

Genome-wide identification of poplar GSTU gene family and its PtrGSTU23 and PtrGSTU40 to improve salt tolerance in poplar

Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?

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