The Cluster Transfer Function of AtNEET Supports the Ferredoxin–Thioredoxin Network of Plant Cells

Sara I. Zandalinas, Luhua Song, Rachel Nechushtai, David G. Mendoza-Cozatl, Ron Mittler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

NEET proteins are conserved 2Fe-2S proteins that regulate the levels of iron and reactive oxygen species in plant and mammalian cells. Previous studies of seedlings with constitutive expression of AtNEET, or its dominant-negative variant H89C (impaired in 2Fe-2S cluster transfer), revealed that disrupting AtNEET function causes oxidative stress, chloroplast iron overload, activation of iron-deficiency responses, and cell death. Because disrupting AtNEET function is deleterious to plants, we developed an inducible expression system to study AtNEET function in mature plants using a time-course proteomics approach. Here, we report that the suppression of AtNEET cluster transfer function results in drastic changes in the expression of different members of the ferredoxin (Fd), Fd-thioredoxin (TRX) reductase (FTR), and TRX network of Arabidopsis, as well as in cytosolic cluster assembly proteins. In addition, the expression of Yellow Stripe-Like 6 (YSL6), involved in iron export from chloroplasts was elevated. Taken together, our findings reveal new roles for AtNEET in supporting the Fd-TFR-TRX network of plants, iron mobilization from the chloroplast, and cytosolic 2Fe-2S cluster assembly. In addition, we show that the AtNEET function is linked to the expression of glutathione peroxidases (GPXs), which play a key role in the regulation of ferroptosis and redox balance in different organisms.

Original languageAmerican English
Article number1533
JournalAntioxidants
Volume11
Issue number8
DOIs
StatePublished - Aug 2022

Bibliographical note

Publisher Copyright:
© 2022 by the authors.

Keywords

  • NEET
  • ROS
  • arabidopsis
  • chloroplast
  • inducible expression
  • iron–sulfur
  • proteomics
  • thioredoxin

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