JAZ repressor proteins are targets of the SCFCOI1 complex during jasmonate signalling

Bryan Thines, Leron Katsir, Maeli Melotto, Yajie Niu, Ajin Mandaokar, Guanghui Liu, Kinya Nomura, Sheng Yang He, Gregg A. Howe and John Browse ()
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Bryan Thines: Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA
Leron Katsir: Department of Energy-Plant Research Laboratory,
Maeli Melotto: Department of Energy-Plant Research Laboratory,
Yajie Niu: Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA
Ajin Mandaokar: Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA
Guanghui Liu: Department of Energy-Plant Research Laboratory,
Kinya Nomura: Department of Energy-Plant Research Laboratory,
Sheng Yang He: Department of Energy-Plant Research Laboratory,
Gregg A. Howe: Department of Energy-Plant Research Laboratory,
John Browse: Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA

Nature, 2007, vol. 448, issue 7154, 661-665

Abstract: Abstract Jasmonate and related signalling compounds have a crucial role in both host immunity and development in plants, but the molecular details of the signalling mechanism are poorly understood. Here we identify members of the jasmonate ZIM-domain (JAZ) protein family as key regulators of jasmonate signalling. JAZ1 protein acts to repress transcription of jasmonate-responsive genes. Jasmonate treatment causes JAZ1 degradation and this degradation is dependent on activities of the SCFCOI1 ubiquitin ligase and the 26S proteasome. Furthermore, the jasmonoyl–isoleucine (JA–Ile) conjugate, but not other jasmonate-derivatives such as jasmonate, 12-oxo-phytodienoic acid, or methyl-jasmonate, promotes physical interaction between COI1 and JAZ1 proteins in the absence of other plant proteins. Our results suggest a model in which jasmonate ligands promote the binding of the SCFCOI1 ubiquitin ligase to and subsequent degradation of the JAZ1 repressor protein, and implicate the SCFCOI1–JAZ1 protein complex as a site of perception of the plant hormone JA–Ile.

Date: 2007
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DOI: 10.1038/nature05960

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