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Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis

Author

Listed:
  • Eric Linster

    (Centre for Organismal Studies, University of Heidelberg
    Hartmut Hoffmann-Berling International Graduate School, University of Heidelberg)

  • Iwona Stephan

    (Centre for Organismal Studies, University of Heidelberg)

  • Willy V. Bienvenut

    (Institute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud)

  • Jodi Maple-Grødem

    (Center for Organelle Research, University of Stavanger)

  • Line M. Myklebust

    (University of Bergen)

  • Monika Huber

    (Centre for Organismal Studies, University of Heidelberg
    Hartmut Hoffmann-Berling International Graduate School, University of Heidelberg)

  • Michael Reichelt

    (Max Planck institute for Chemical Ecology)

  • Carsten Sticht

    (Center for Medical Research)

  • Simon Geir Møller

    (Center for Organelle Research, University of Stavanger
    St John’s University
    Norwegian Centre for Movement Disorders, Stavanger University Hospital)

  • Thierry Meinnel

    (Institute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud)

  • Thomas Arnesen

    (University of Bergen
    Haukeland University Hospital)

  • Carmela Giglione

    (Institute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud)

  • Rüdiger Hell

    (Centre for Organismal Studies, University of Heidelberg)

  • Markus Wirtz

    (Centre for Organismal Studies, University of Heidelberg)

Abstract

N-terminal acetylation (NTA) catalysed by N-terminal acetyltransferases (Nats) is among the most common protein modifications in eukaryotes, but its significance is still enigmatic. Here we characterize the plant NatA complex and reveal evolutionary conservation of NatA biochemical properties in higher eukaryotes and uncover specific and essential functions of NatA for development, biosynthetic pathways and stress responses in plants. We show that NTA decreases significantly after drought stress, and NatA abundance is rapidly downregulated by the phytohormone abscisic acid. Accordingly, transgenic downregulation of NatA induces the drought stress response and results in strikingly drought resistant plants. Thus, we propose that NTA by the NatA complex acts as a cellular surveillance mechanism during stress and that imprinting of the proteome by NatA is an important switch for the control of metabolism, development and cellular stress responses downstream of abscisic acid.

Suggested Citation

  • Eric Linster & Iwona Stephan & Willy V. Bienvenut & Jodi Maple-Grødem & Line M. Myklebust & Monika Huber & Michael Reichelt & Carsten Sticht & Simon Geir Møller & Thierry Meinnel & Thomas Arnesen & Ca, 2015. "Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis," Nature Communications, Nature, vol. 6(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8640
    DOI: 10.1038/ncomms8640
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    Cited by:

    1. Charlotte M. François & Thomas Pihl & Marion Dunoyer de Segonzac & Chloé Hérault & Bruno Hudry, 2023. "Metabolic regulation of proteome stability via N-terminal acetylation controls male germline stem cell differentiation and reproduction," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Eric Linster & Francy L. Forero Ruiz & Pavlina Miklankova & Thomas Ruppert & Johannes Mueller & Laura Armbruster & Xiaodi Gong & Giovanna Serino & Matthias Mann & Rüdiger Hell & Markus Wirtz, 2022. "Cotranslational N-degron masking by acetylation promotes proteome stability in plants," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Ulises H. Guzman & Henriette Aksnes & Rasmus Ree & Nicolai Krogh & Magnus E. Jakobsson & Lars J. Jensen & Thomas Arnesen & Jesper V. Olsen, 2023. "Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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