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

Mark D. White, Maria Klecker, Richard J. Hopkinson, Daan Weits, Carolin Mueller, Christin Naumann, Rebecca O’Neill, James Wickens, Tom N. Grossmann, Nico Dissmeyer, Emily Flashman
doi: https://doi.org/10.1101/069336
Mark D. White
1Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
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Maria Klecker
2Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany
3ScienceCampus Halle – Plant-based Bioeconomy, Betty-Heimann-Str. 3, D-06120 Halle (Saale), Germany
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Richard J. Hopkinson
1Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
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Daan Weits
4Institute of Biology I, RWTH Aachen University, Worringerweg 1, D-52074 Aachen, Germany
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Carolin Mueller
5Chemical Genomics Centre of the Max Planck Society, Department of Chemistry and Chemical Biology, Technische Universität Dortmund, Otto-Hahn-Str. 15, D-44227 Dortmund, Germany
6VU University Amsterdam, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands
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Christin Naumann
2Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany
3ScienceCampus Halle – Plant-based Bioeconomy, Betty-Heimann-Str. 3, D-06120 Halle (Saale), Germany
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Rebecca O’Neill
1Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
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James Wickens
1Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
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Tom N. Grossmann
5Chemical Genomics Centre of the Max Planck Society, Department of Chemistry and Chemical Biology, Technische Universität Dortmund, Otto-Hahn-Str. 15, D-44227 Dortmund, Germany
6VU University Amsterdam, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands
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Nico Dissmeyer
2Independent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany
3ScienceCampus Halle – Plant-based Bioeconomy, Betty-Heimann-Str. 3, D-06120 Halle (Saale), Germany
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  • For correspondence: emily.flashman@chem.ox.ac.uk nico.dissmeyer@ipb-halle.de
Emily Flashman
1Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom
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  • For correspondence: emily.flashman@chem.ox.ac.uk nico.dissmeyer@ipb-halle.de
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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 the 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 catalysing 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 cysteine oxidation 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.

Abbreviations PCO, plant cysteine oxidase; ATE, arginyl tRNA transferase; ERF-VII, group VII ETHYLENE RESPONSE FACTOR; 2OG, 2-oxoglutarate; NMR, nuclear magnetic resonance; Met, methionine; NME, N-terminal Met excision; Nt, N-terminal; NO, nitric oxide; HIF, hypoxia-inducible factor; PHD, prolyl hydroxylase; MALDI-MS, matrix-assisted laser desorption/ionization-mass spectrometry; LC-MS, liquid chromatography-mass spectrometry; HRE, HYPOXIA RESPONSIVE ERF; RAP, RELATED TO APETALA2; EBP, ETHYLENE RESPONSE FACTOR 72; CDO, cysteine dioxygenase; MAP, Met-aminopeptidase.

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Posted August 14, 2016.
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Plant Cysteine Oxidases are Dioxygenases that Directly Enable Arginyl Transferase-Catalyzed Arginylation of N-End Rule Targets
Mark D. White, Maria Klecker, Richard J. Hopkinson, Daan Weits, Carolin Mueller, Christin Naumann, Rebecca O’Neill, James Wickens, Tom N. Grossmann, Nico Dissmeyer, Emily Flashman
bioRxiv 069336; doi: https://doi.org/10.1101/069336
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Plant Cysteine Oxidases are Dioxygenases that Directly Enable Arginyl Transferase-Catalyzed Arginylation of N-End Rule Targets
Mark D. White, Maria Klecker, Richard J. Hopkinson, Daan Weits, Carolin Mueller, Christin Naumann, Rebecca O’Neill, James Wickens, Tom N. Grossmann, Nico Dissmeyer, Emily Flashman
bioRxiv 069336; doi: https://doi.org/10.1101/069336

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