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

Authors :
Emily Flashman
Rebecca O’Neill
Elspeth F. Garman
Nico Dissmeyer
Daan A. Weits
Richard J. Hopkinson
Tom N. Grossmann
Jiayu Yang
James Wickens
Maria Klecker
Jonathan C. Brooks-Bartlett
Christin Naumann
Mark D. White
Carolin Mueller
Organic Chemistry
AIMMS
Source :
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017), Nature Communications, 8:14690. Nature Publishing Group, Nature Communications 8, 14690 (2017). doi:10.1038/ncomms14690, Nature Communications, White, M D, Klecker, M, Hopkinson, R J, Weits, D A, Mueller, C, Naumann, C, O'Neill, R, Wickens, J, Yang, J, Brooks-Bartlett, J C, Garman, E F, Grossmann, T N, Dissmeyer, N & Flashman, E 2017, ' Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets ', Nature Communications, vol. 8, 14690, pp. 14690 . https://doi.org/10.1038/ncomms14690
Publication Year :
2017
Publisher :
Nature Portfolio, 2017.

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.<br />The N-end rule pathway targets substrate proteins for proteasomal degradation. Here, White et al. show that Arabidopsis PLANT CYSTEINE OXIDASEs show dioxygenase activity producing Cys-sulfinic acid at the N-terminus of target proteins, which then act as direct substrates for arginyl transferase.

Details

Language :
English
ISSN :
20411723
Volume :
8
Issue :
1
Database :
OpenAIRE
Journal :
Nature Communications
Accession number :
edsair.doi.dedup.....f8ea0ac2182dfa82785549fcc2dd73d3
Full Text :
https://doi.org/10.1038/ncomms14690