Plant Cysteine Oxidases are Dioxygenases that Directly Enable Arginyl Transferase-Catalyzed Arginylation of N-End Rule Targets (original) (raw)

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, Maria Klecker, Richard J. Hopkinson, Daan Weits, Carolin Mueller, Christin Naumann, Rebecca O’Neill, James Wickens, Jiayu Yang, Jonathan C. Brooks-Bartlett, Elspeth F. Garman, Tom N. Grossman, Nico Dissmeyer, Emily Flashman

doi: https://doi.org/10.1101/069336

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Abstract

Crop yield loss due to flooding is a threat to food security. Submergence-induced hypoxia in plants results in stabilisation of group VII ETHYLENE RESPONSE FACTORS (ERF-VIIs), which aid survival under these adverse conditions. ERF-VII stability is controlled by the N-end rule pathway, which proposes that ERF-VII N-terminal cysteine oxidation in normoxia enables arginylation followed by proteasomal degradation. The PLANT CYSTEINE OXIDASEs (PCOs) have been identified as catalysts of this oxidation. ERF-VII stabilisation in hypoxia presumably arises from reduced PCO activity. We directly demonstrate that PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This is the first molecular evidence showing N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and the first ATE1 substrate in plants. The PCOs and ATE1 may be viable intervention targets to stabilise N-end rule substrates, including ERF-VIIs to enhance submergence tolerance in agronomy.

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