Journal
NATURE
Volume 468, Issue 7322, Pages 400-U301Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature09430
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Funding
- Howard Hughes Medical Institute
- National Institutes of Health [R01 CA107134, T32 GM07270, R01GM57795, R01AI068718]
- National Science Foundation [0929100]
- US Department of Energy [DE-FG02-99ER20323, DE-FG02-91ER20021]
- Michigan State University
- Welch Foundation [I-1304]
- European Research Council (ERC) under the European Community [239679]
- European Research Council (ERC) [239679] Funding Source: European Research Council (ERC)
- U.S. Department of Energy (DOE) [DE-FG02-99ER20323] Funding Source: U.S. Department of Energy (DOE)
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Jasmonates are a family of plant hormones that regulate plant growth, development and responses to stress. The F-box protein CORONATINE INSENSITIVE 1 (COI1) mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JAZ proteins. Despite its importance, the mechanism of jasmonate perception remains unclear. Here we present structural and pharmacological data to show that the true Arabidopsis jasmonate receptor is a complex of both COI1 and JAZ. COI1 contains an open pocket that recognizes the bioactive hormone (3R, 7S)-jasmonoyl-L-isoleucine (JA-Ile) with high specificity. High-affinity hormone binding requires a bipartite JAZ degron sequence consisting of a conserved a-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 jasmonate co-receptor complex, inositol pentakisphosphate, which interacts with both COI1 and JAZ adjacent to the ligand. Our results unravel the mechanism of jasmonate perception and highlight the ability of F-box proteins to evolve as multi-component signalling hubs.
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