Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence

Daniel Marino, Solène Froidure, Joanne Canonne, Sara Ben Khaled, Mehdi Khafif, Cécile Pouzet, Alain Jauneau, Dominique Roby and Susana Rivas ()
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Daniel Marino: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441
Solène Froidure: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441
Joanne Canonne: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441
Sara Ben Khaled: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441
Mehdi Khafif: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441
Cécile Pouzet: Fédération de Recherche 3450, Plateforme Imagerie, Pôle de Biotechnologie Végétale
Alain Jauneau: Fédération de Recherche 3450, Plateforme Imagerie, Pôle de Biotechnologie Végétale
Dominique Roby: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441
Susana Rivas: INRA, Laboratoire des Interactions Plantes-Microorganismes, UMR441

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract One of the most efficient plant resistance reactions to pathogen attack is the hypersensitive response, a form of programmed cell death at infection sites. The Arabidopsis transcription factor MYB30 is a positive regulator of hypersensitive cell death responses. Here we show that MIEL1 (MYB30-Interacting E3 Ligase1), an Arabidopsis RING-type E3 ubiquitin ligase that interacts with and ubiquitinates MYB30, leads to MYB30 proteasomal degradation and downregulation of its transcriptional activity. In non-infected plants, MIEL1 attenuates cell death and defence through degradation of MYB30. Following bacterial inoculation, repression of MIEL1 expression removes this negative regulation allowing sufficient MYB30 accumulation in the inoculated zone to trigger the hypersensitive response and restrict pathogen growth. Our work underlines the important role played by ubiquitination to control the hypersensitive response and highlights the sophisticated fine-tuning of plant responses to pathogen attack. Overall, this work emphasizes the importance of protein modification by ubiquitination during the regulation of transcriptional responses to stress in eukaryotic cells.

Date: 2013
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DOI: 10.1038/ncomms2479

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