Evidence map›Paper›PMID 28332493›Full record

ArticleNature communications2017

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 and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
49.2field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

123 citing papers in PubMed, 250 citations in OpenAlex.

  1. Article
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  5. HNature · 2026
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  8. The next frontier: Exploring plant hypoxia sensing and response mechanisms through synthetic biology.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Article
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  12. Plastid-to-nucleus communication under hypoxia involves group VII ethylene response factors inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Article
  14. Review
  15. Review
  16. Nitric oxide promotes cysteine N-degron proteolysis through control of oxygen availability.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Oxygen sensing and plant adaptation to flooding in a changing climate.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  20. Article

63 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 3 countries.

Mark D WhiteChemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Maria KleckerIndependent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany.
Richard J HopkinsonChemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Daan A WeitsInstitute of Biology I, RWTH Aachen University, Worringerweg 1, D-52074 Aachen, Germany.
Carolin MuellerChemical Genomics Centre of the Max Planck Society, Otto-Hahn-Strasse 15, D-44227 Dortmund, Germany.
Christin NaumannIndependent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany.
Rebecca O'NeillChemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
James WickensChemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Jiayu YangChemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Jonathan C Brooks-BartlettDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Elspeth F GarmanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Tom N GrossmannChemical Genomics Centre of the Max Planck Society, Otto-Hahn-Strasse 15, D-44227 Dortmund, Germany.
Nico DissmeyerIndependent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, D-06120 Halle (Saale), Germany.ORCID 0000-0002-4156-3761
Emily FlashmanChemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
University of Oxford · GBHalle Institute for Economic Research · DEMax Planck Society · DERWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Amino Acid SequenceAminoacyltransferasesArabidopsisArabidopsis ProteinsArginineBiocatalysisCysteineCysteine DioxygenaseDioxygenasesIsoenzymesOxidation-ReductionOxygenAminoacyltransferasesArabidopsis ProteinsArgininearginyltransferaseCysteineCysteine DioxygenaseDioxygenasesIsoenzymesOxygen

Identifiers

PMID28332493
PMCPMC5376641
OpenAlexW2952647141

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.