title: Regulation and function of Arabidopsis JASMONATE ZIM-domain genes in response to wounding and herbivory.
abstract: Jasmonate (JA) and its amino acid conjugate, jasmonoyl-isoleucine (JA-Ile), play important roles in regulating plant defense responses to insect herbivores. Recent studies indicate that JA-Ile promotes the degradation of JASMONATE ZIM-domain (JAZ) transcriptional repressors through the activity of the E(3) ubiquitin-ligase SCF(COI1). Here, we investigated the regulation and function of JAZ genes during the interaction of Arabidopsis (Arabidopsis thaliana) with the generalist herbivore Spodoptera exigua. Most members of the JAZ gene family were highly expressed in response to S. exigua feeding and mechanical wounding. JAZ transcript levels increased within 5 min of mechanical tissue damage, coincident with a large (approximately 25-fold) rise in JA and JA-Ile levels. Wound-induced expression of JAZ and other CORONATINE-INSENSITIVE1 (COI1)-dependent genes was not impaired in the jar1-1 mutant that is partially deficient in the conversion of JA to JA-Ile. Experiments performed with the protein synthesis inhibitor cycloheximide provided evidence that JAZs, MYC2, and genes encoding several JA biosynthetic enzymes are primary response genes whose expression is derepressed upon COI1-dependent turnover of a labile repressor protein(s). We also show that overexpression of a modified form of JAZ1 (JAZ1Delta3A) that is stable in the presence of JA compromises host resistance to feeding by S. exigua larvae. These findings establish a role for JAZ proteins in the regulation of plant anti-insect defense, and support the hypothesis that JA-Ile and perhaps other JA derivatives activate COI1-dependent wound responses in Arabidopsis. Our results also indicate that the timing of JA-induced transcription in response to wounding is more rapid than previously realized.
authors.affiliation: Department of Energy Plant Research Laboratory , Michigan State University, East Lansing, MI 48824, USA.
authors.forename: Hoo Sun
authors.initials: HS
authors.lastname: Chung
authors.forename: Abraham J K
authors.initials: AJ
authors.lastname: Koo
authors.forename: Xiaoli
authors.initials: X
authors.lastname: Gao
authors.forename: Sastry
authors.initials: S
authors.lastname: Jayanty
authors.forename: Bryan
authors.initials: B
authors.lastname: Thines
authors.forename: A Daniel
authors.initials: AD
authors.lastname: Jones
authors.forename: Gregg A
authors.initials: GA
authors.lastname: Howe
mesh_terms: D000222:Adaptation, Physiological; D000818:Animals; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000469:parasitology; D029681:Arabidopsis Proteins / Q000378:metabolism; D051778:Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / Q000378:metabolism; D003513:Cycloheximide; D003517:Cyclopentanes / Q000378:metabolism; D005247:Feeding Behavior / Q000502:physiology; D018506:Gene Expression Regulation, Plant; D006790:Host-Parasite Interactions / Q000502:physiology*; D007814:Larva / Q000502:physiology; D005810:Multigene Family; D009713:Nucleotidyltransferases / Q000378:metabolism; D054883:Oxylipins / Q000378:metabolism; D011500:Protein Synthesis Inhibitors; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D044843:SKP Cullin F-Box Protein Ligases / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D018411:Spodoptera / Q000502:physiology*; D010453:Peptide Synthases
chemical_list: D029681:Arabidopsis Proteins; D051778:Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; D003513:Cycloheximide; D003517:Cyclopentanes; D009713:Nucleotidyltransferases; D054883:Oxylipins; D011500:Protein Synthesis Inhibitors; D012097:Repressor Proteins; D044843:SKP Cullin F-Box Protein Ligases; C112279:COI1 protein, Arabidopsis; C473611:MYC2 protein, Arabidopsis; C011006:jasmonic acid; C412831:AT2G46370 protein, Arabidopsis; D010453:Peptide Synthases