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<p>Glutathione transferases (GSTs, EC 2.5.1.18) are a diverse enzyme family involved in various cellular processes, regulated by several stimuli, including plant hormones (phytohormones). Additionally, GSTs can also influence hormone levels, as certain GSTs, particularly members of the Phi class GSTs (GSTFs) have been reported to directly bind small phytohormones (auxin, cytokinin, and salicylic acid). However, the structural aspects of these interactions remained unresolved. It has been documented that an <i>Arabidopsis thaliana</i> GSTF, AtGSTF2, possesses unique non-catalytic ligand-binding sites (L sites). This study focuses on the orthologous tomato (<i>Solanum lycopersicum</i>) GSTFs (SlGSTFs) and explores the connection between this non-catalytic ligand-binding function and phytohormones. Using modern <i>in silico</i> techniques, such as protein modelling by AlphaFold, molecular docking, and molecular dynamics (MD) simulations, we provide the first insights into the possible phytohormone-binding ability of SlGSTFs. In particular, SlGSTF5 shows significant potential for a novel phytohormone binding function, thereby broadening the potential roles of plant GSTs. Our work also includes a simple protocol for modelling and analysing protein-ligand interactions, offering valuable insights into the role of individual plant GSTs.</p>

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The non-catalytic binding of auxin, cytokinin and salicylic acid by tomato Phi class glutathione transferases: insights from computational modelling

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月3日

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  • Ádám Barnabás Hajnal,
  • Ágnes Gallé,
  • Jolán Csiszár

摘要

Glutathione transferases (GSTs, EC 2.5.1.18) are a diverse enzyme family involved in various cellular processes, regulated by several stimuli, including plant hormones (phytohormones). Additionally, GSTs can also influence hormone levels, as certain GSTs, particularly members of the Phi class GSTs (GSTFs) have been reported to directly bind small phytohormones (auxin, cytokinin, and salicylic acid). However, the structural aspects of these interactions remained unresolved. It has been documented that an Arabidopsis thaliana GSTF, AtGSTF2, possesses unique non-catalytic ligand-binding sites (L sites). This study focuses on the orthologous tomato (Solanum lycopersicum) GSTFs (SlGSTFs) and explores the connection between this non-catalytic ligand-binding function and phytohormones. Using modern in silico techniques, such as protein modelling by AlphaFold, molecular docking, and molecular dynamics (MD) simulations, we provide the first insights into the possible phytohormone-binding ability of SlGSTFs. In particular, SlGSTF5 shows significant potential for a novel phytohormone binding function, thereby broadening the potential roles of plant GSTs. Our work also includes a simple protocol for modelling and analysing protein-ligand interactions, offering valuable insights into the role of individual plant GSTs.