Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets

Mark D. White, Maria Klecker, Richard J. Hopkinson, Daan A. Weits, Carolin Mueller, Christin Naumann, Rebecca O’Neill, James Wickens, Jiayu Yang, Jonathan C. Brooks-Bartlett, Elspeth F. Garman, Tom N. Grossmann, Nico Dissmeyer () and Emily Flashman ()
Additional contact information
Mark D. White: Chemistry Research Laboratory, University of Oxford
Maria Klecker: Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB)
Richard J. Hopkinson: Chemistry Research Laboratory, University of Oxford
Daan A. Weits: Institute of Biology I, RWTH Aachen University
Carolin Mueller: Chemical Genomics Centre of the Max Planck Society
Christin Naumann: Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB)
Rebecca O’Neill: Chemistry Research Laboratory, University of Oxford
James Wickens: Chemistry Research Laboratory, University of Oxford
Jiayu Yang: Chemistry Research Laboratory, University of Oxford
Jonathan C. Brooks-Bartlett: University of Oxford
Elspeth F. Garman: University of Oxford
Tom N. Grossmann: Chemical Genomics Centre of the Max Planck Society
Nico Dissmeyer: Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB)
Emily Flashman: Chemistry Research Laboratory, University of Oxford

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract Crop yield loss due to flooding is a threat to food security. Submergence-induced hypoxia in plants results in stabilization 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 stabilization 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 provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. The PCOs and ATE1 may be viable intervention targets to stabilize N-end rule substrates, including ERF-VIIs, to enhance submergence tolerance in agriculture.

Date: 2017
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DOI: 10.1038/ncomms14690

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