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JAZ repressor proteins are targets of the SCF(COI1) complex during jasmonate signalling.
- Source :
-
Nature [Nature] 2007 Aug 09; Vol. 448 (7154), pp. 661-5. Date of Electronic Publication: 2007 Jul 18. - Publication Year :
- 2007
-
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 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.
- Subjects :
- Amino Acid Sequence
Arabidopsis genetics
Arabidopsis Proteins chemistry
Arabidopsis Proteins genetics
Cell-Free System
Genes, Plant genetics
Glucuronidase genetics
Glucuronidase metabolism
Isoleucine pharmacology
Molecular Sequence Data
Multigene Family genetics
Oxylipins
Phenotype
Protein Binding
Protein Structure, Tertiary
Repressor Proteins chemistry
Repressor Proteins genetics
Substrate Specificity
Arabidopsis drug effects
Arabidopsis metabolism
Arabidopsis Proteins metabolism
Cyclopentanes pharmacology
Isoleucine analogs & derivatives
Repressor Proteins metabolism
SKP Cullin F-Box Protein Ligases metabolism
Signal Transduction drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 1476-4687
- Volume :
- 448
- Issue :
- 7154
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 17637677
- Full Text :
- https://doi.org/10.1038/nature05960