Nitric oxide-mediated S-nitrosylation of IAA17 protein in intrinsically disordered region represses auxin signaling

Hongwei Jing, Xiaolu Yang, Ryan J. Emenecker, Jian Feng, Jian Zhang, Marcelo Rodrigues Alves de Figueiredo, Patarasuda Chaisupa, R. Clay Wright, Alex S. Holehouse, Lucia C. Strader, Jianru Zuo

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The phytohormone auxin plays crucial roles in nearly every aspect of plant growth and development. Auxin signaling is activated through the phytohormone-induced proteasomal degradation of the Auxin/INDOLE-3-ACETIC ACID (Aux/IAA) family of transcriptional repressors. Notably, many auxin-modulated physiological processes are also regulated by nitric oxide (NO) that executes its biological effects predominantly through protein S-nitrosylation at specific cysteine residues. However, little is known about the molecular mechanisms in regulating the interactive NO and auxin networks. Here, we show that NO represses auxin signaling by inhibiting IAA17 protein degradation. NO induces the S-nitrosylation of Cys-70 located in the intrinsically disordered region of IAA17, which inhibits the TIR1–IAA17 interaction and consequently the proteasomal degradation of IAA17. The accumulation of a higher level of IAA17 attenuates auxin response. Moreover, an IAA17C70W nitrosomimetic mutation renders the accumulation of a higher level of the mutated protein, thereby causing partial resistance to auxin and defective lateral root development. Taken together, these results suggest that S-nitrosylation of IAA17 at Cys-70 inhibits its interaction with TIR1, thereby negatively regulating auxin signaling. This study provides unique molecular insights into the redox-based auxin signaling in regulating plant growth and development.

Original languageEnglish
Pages (from-to)473-485
Number of pages13
JournalJournal of Genetics and Genomics
Volume50
Issue number7
DOIs
StatePublished - Jul 2023

Keywords

  • Arabidopsis thaliana
  • Aux/IAA
  • Auxin
  • Intrinsically disordered region
  • Nitric oxide
  • S-nitrosylation

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