Arabidopsis thaliana 3-mercaptopyruvate sulfurtransferases interact with and are protected by reducing systems.

Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE

Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology

Sulfurtransferases/*metabolism; Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Catalysis ; Catalytic Domain ; Disulfides ; Glutathione/analogs & derivatives ; Hydrogen Sulfide/metabolism ; Kinetics ; Oxidation-Reduction ; Sulfur/metabolism ; Sulfurtransferases/genetics ; Sulfurtransferases/physiology

The formation of a persulfide group (-SSH) on cysteine residues has gained attention as a reversible posttranslational modification contributing to protein regulation or protection. The widely distributed 3-mercaptopyruvate sulfurtransferases (MSTs) are implicated in the generation of persulfidated molecules and H 2 S biogenesis through transfer of a sulfane sulfur atom from a suitable donor to an acceptor. Arabidopsis has two MSTs, named STR1 and STR2, but they are poorly characterized. To learn more about these enzymes, we conducted a series of biochemical experiments including a variety of possible reducing systems. Our kinetic studies, which used a combination of sulfur donors and acceptors revealed that both MSTs use 3-mercaptopyruvate efficiently as a sulfur donor while thioredoxins, glutathione, and glutaredoxins all served as high-affinity sulfane sulfur acceptors. Using the redox-sensitive GFP (roGFP2) as a model acceptor protein, we showed that the persulfide-forming MSTs catalyze roGFP2 oxidation and more generally trans-persulfidation reactions. However, a preferential interaction with the thioredoxin system and glutathione was observed in case of competition between these sulfur acceptors. Moreover, we observed that MSTs are sensitive to overoxidation but are protected from an irreversible inactivation by their persulfide intermediate and subsequent reactivation by thioredoxins or glutathione. This work provides significant insights into Arabidopsis STR1 and STR2 catalytic properties and more specifically emphasizes the interaction with cellular reducing systems for the generation of H 2 S and glutathione persulfide and reactivation of an oxidatively modified form.
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the content of this article.
(Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)

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Keywords: 3-mercaptopyruvate; cysteine; glutathione; hydrogen sulfide; persulfide; sulfurtransferase; thioredoxin

0 (Arabidopsis Proteins)
0 (Disulfides)
0 (glutathione persulfide)
70FD1KFU70 (Sulfur)
EC 2.8.1.- (Sulfurtransferases)
EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase)
GAN16C9B8O (Glutathione)
YY9FVM7NSN (Hydrogen Sulfide)

Date Created: 20210220 Date Completed: 20210827 Latest Revision: 20210827

20221213

PMC7995614

10.1016/j.jbc.2021.100429

33609525