Jasmonate perception by inositol phosphate-potentiated COI1-JAZ co-receptor

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Abstract

Jasmonates (JAs) are a family of plant hormones that regulate plant growth, development, and responses to stress. The F-box protein CORONATINE-INSENSITIVE 1 (COI1) mediates JA signaling by promoting hormone-dependent ubiquitination and degradation of transcriptional repressor JAZ proteins. Despite its importance, the mechanism of JA perception remains unclear. Here we present structural and pharmacological data to show that the true JA receptor is a complex of both COI1 and JAZ. COI1 contains an open pocket that recognizes the bioactive hormone, (3 R,7 S)-jasmonoyl-L-isoleucine (JA-Ile), with high specificity. High-affinity hormone binding requires a bipartite JAZ degron sequence consisting of a conserved α-helix for COI1 docking and a loop region to trap the hormone in its binding pocket. In addition, we identify a third critical component of the JA co-receptor complex, inositol pentakisphosphate, which interacts with both COI1 and JAZ adjacent to the ligand. Our results unravel the mechanism of JA perception and highlight the ability of F-box proteins to evolve as multi-component signaling hubs.

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Most cited references 24

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JAZ repressor proteins are targets of the SCF(COI1) complex during jasmonate signalling.

Bryan C. Thines, Leron Katsir, Maeli Melotto … (2007)

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 SCF(COI1) 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 SCF(COI1) ubiquitin ligase to and subsequent degradation of the JAZ1 repressor protein, and implicate the SCF(COI1)-JAZ1 protein complex as a site of perception of the plant hormone JA-Ile.

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Improved methods for building protein models in electron density maps and the location of errors in these models.

T. Jones, J. Y. Zou, S Cowan … (1991)

Map interpretation remains a critical step in solving the structure of a macromolecule. Errors introduced at this early stage may persist throughout crystallographic refinement and result in an incorrect structure. The normally quoted crystallographic residual is often a poor description for the quality of the model. Strategies and tools are described that help to alleviate this problem. These simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.

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JASMONATE-INSENSITIVE1 encodes a MYC transcription factor essential to discriminate between different jasmonate-regulated defense responses in Arabidopsis.

Óscar Lorenzo, Jose M Chico, José Sánchez-Serrano … (2004)

In spite of the importance of jasmonates (JAs) as plant growth and stress regulators, the molecular components of their signaling pathway remain largely unknown. By means of a genetic screen that exploits the cross talk between ethylene (ET) and JAs, we describe the identification of several new loci involved in JA signaling and the characterization and positional cloning of one of them, JASMONATE-INSENSITIVE1 (JAI1/JIN1). JIN1 encodes AtMYC2, a nuclear-localized basic helix-loop-helix-leucine zipper transcription factor, whose expression is rapidly upregulated by JA, in a CORONATINE INSENSITIVE1-dependent manner. Gain-of-function experiments confirmed the relevance of AtMYC2 in the activation of JA signaling. AtMYC2 differentially regulates the expression of two groups of JA-induced genes. The first group includes genes involved in defense responses against pathogens and is repressed by AtMYC2. Consistently, jin1 mutants show increased resistance to necrotrophic pathogens. The second group, integrated by genes involved in JA-mediated systemic responses to wounding, is activated by AtMYC2. Conversely, Ethylene-Response-Factor1 (ERF1) positively regulates the expression of the first group of genes and represses the second. These results highlight the existence of two branches in the JA signaling pathway, antagonistically regulated by AtMYC2 and ERF1, that are coincident with the alternative responses activated by JA and ET to two different sets of stresses, namely pathogen attack and wounding.

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Author and article information

Journal

Journal ID (nlm-journal-id): 0410462

Journal ID (pubmed-jr-id): 6011

Journal ID (nlm-ta): Nature

Title: Nature

ISSN (Print): 0028-0836

ISSN (Electronic): 1476-4687

Publication date Nihms-submitted: 24 August 2010

Publication date (Electronic): 6 October 2010

Publication date (Print): 18 November 2010

Publication date PMC-release: 18 May 2011

Volume: 468

Issue: 7322

Pages: 400-405

Affiliations

[1 ]Department of Pharmacology, University of Washington, Seattle, Washington 98195, USA

[2 ]Howard Hughes Medical Institute, Box 357280, University of Washington, Seattle, Washington 98195, USA

[3 ]Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, USA

[4 ]Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824, USA

[5 ]Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA

[6 ]Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel

[7 ]Department of Biological Engineering, Tokyo Institute of Technology, 4259-B52 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan 4259

[8 ]Mass Spectrometry Resource, Division of Endocrinology, Diabetes, Metabolism, and Lipid research, Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri, USA

[9 ]Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA

[10 ]Department of Biochemistry, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, Texas 75390, USA

Author notes

Correspondence and requests for materials should be addressed to N.Z. ( nzheng@ 123456u.washington.edu )

[†]

Present address: Department of Genetics, Center for Genetics and Genomics, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115, USA

[*]

These authors contributed equally to this work.

Article

Manuscript ID: nihpa230784

DOI: 10.1038/nature09430

PMC ID: 2988090

PubMed ID: 20927106

SO-VID: b12e492e-1a54-4035-8489-d2c7e3693e61

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