RT Journal Article SR Electronic T1 Plant Cysteine Oxidases are Dioxygenases that Directly Enable Arginyl Transferase-Catalyzed Arginylation of N-End Rule Targets JF bioRxiv FD Cold Spring Harbor Laboratory SP 069336 DO 10.1101/069336 A1 Mark D. White A1 Maria Klecker A1 Richard J. Hopkinson A1 Daan Weits A1 Carolin Mueller A1 Christin Naumann A1 Rebecca O’Neill A1 James Wickens A1 Jiayu Yang A1 Jonathan C. Brooks-Bartlett A1 Elspeth F. Garman A1 Tom N. Grossman A1 Nico Dissmeyer A1 Emily Flashman YR 2016 UL http://biorxiv.org/content/early/2016/12/09/069336.abstract AB 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.