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Structural analysis of the woodland strawberry COI1-JAZ1 co-receptor for the plant hormone jasmonoyl-isoleucine

dc.contributor.authorValenzuela-Riffo F.
dc.contributor.authorGarrido-Bigotes A.
dc.contributor.authorFigueroa P.M.
dc.contributor.authorMorales-Quintana L.
dc.contributor.authorFigueroa C.R.
dc.date.accessioned2020-09-02T22:29:54Z
dc.date.available2020-09-02T22:29:54Z
dc.date.issued2018
dc.identifier10.1016/j.jmgm.2018.09.004
dc.identifier.citation85, , 250-261
dc.identifier.issn10933263
dc.identifier.urihttps://hdl.handle.net/20.500.12728/6507
dc.descriptionThe phytohormone jasmonoyl-isoleucine (JA-Ile) regulates fundamental plant processes. Fragaria vesca, the woodland strawberry, is a model plant for the Rosaceae family, in which the JA-Ile perception is poorly understood at the molecular level. JA-Ile promotes binding of JAZ repressor to COI1 protein in Arabidopsis to activate jasmonate (JA)-dependent responses. The aim of this work was to understand the molecular basis of the interaction between the F. vesca COI1 (FvCOI1) and JAZ1 (FvJAZ1) promoted by JA-Ile using a computational approach. Multiple sequence alignments and phylogenetic analyses of amino acid sequences were performed for FvCOI1, FvJAZ1 and their ortholog sequences. 3D structures for FvCOI1 and FvJAZ1 proteins were built by methods of homology modeling, using AtCOI1-JA-Ile-AtJAZ1 as template and then they were further refined and validated by molecular dynamics (MD) simulation. A molecular docking approach along with MDS analysis were used to gain insights into the interaction between a putative degron-like sequence present in FvJAZ1 with the FvCOI1-JA-Ile complex. FvCOI1 and FvJAZ1 showed high and moderate sequence identity, respectively, with the corresponding ortholog proteins from other plant species including apple, grape, tomato and Arabidopsis. Moreover, the FvJAZ1 has a variant C-terminal IPMQRK sequence instead of the canonical LPIARR degron sequence located in the Jas domain of AtJAZ1. The MD simulation results showed that the FvCOI1-JA-Ile-FvJAZ1 complex was stable, and the IPMQRK peptide of FvJAZ1 directly interacted with FvCOI1 and JA-Ile. The present research provides novel insight into the molecular interactions among key JA-signaling components in the model plant F. vesca, being few examples of characterized JA-Ile receptors at a structural level in plants. © 2018 Elsevier Inc.
dc.language.isoen
dc.publisherElsevier Inc.
dc.subjectCORONATINE INSENSITIVE1 protein
dc.subjectFragaria vesca
dc.subjectJasmonate signaling
dc.subjectJASMONATE ZIM-DOMAIN repressor
dc.subjectJasmonoyl-isoleucine
dc.subjectMolecular dynamics simulations
dc.subjectMolecular modeling
dc.subjectAmino acids
dc.subjectFruits
dc.subjectMolecular modeling
dc.subjectPlants (botany)
dc.subjectProteins
dc.subjectCoronatine
dc.subjectFragaria
dc.subjectJasmonate signaling
dc.subjectJasmonates
dc.subjectJasmonoyl-isoleucine
dc.subjectMolecular dynamics simulations
dc.subjectMolecular dynamics
dc.subjectcoronatine
dc.subjectcoronatine insensitive1 protein
dc.subjectjasmonoyl isoleucine
dc.subjectphytohormone
dc.subjectunclassified drug
dc.subjectcyclopentane derivative
dc.subjectisoleucine
dc.subjectjasmonoyl-isoleucine
dc.subjectligand
dc.subjectmultiprotein complex
dc.subjectphytohormone
dc.subjectplant protein
dc.subjectprotein binding
dc.subjectamino acid sequence
dc.subjectapple
dc.subjectArabidopsis
dc.subjectArabidopsis thaliana
dc.subjectArticle
dc.subjectcontrolled study
dc.subjectfruit ripening
dc.subjectgrape
dc.subjectmolecular docking
dc.subjectmolecular dynamics
dc.subjectmolecular interaction
dc.subjectnonhuman
dc.subjectphylogeny
dc.subjectpriority journal
dc.subjectprotein analysis
dc.subjectprotein conformation
dc.subjectprotein interaction
dc.subjectprotein structure
dc.subjectsequence alignment
dc.subjectstrawberry
dc.subjecttomato
dc.subjectX ray diffraction
dc.subjectchemistry
dc.subjectconformation
dc.subjectDNA sequence
dc.subjectFragaria
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectmolecular model
dc.subjectprotein domain
dc.subjectstructure activity relation
dc.subjectAmino Acid Sequence
dc.subjectCyclopentanes
dc.subjectFragaria
dc.subjectIsoleucine
dc.subjectLigands
dc.subjectModels, Molecular
dc.subjectMolecular Conformation
dc.subjectMultiprotein Complexes
dc.subjectPlant Growth Regulators
dc.subjectPlant Proteins
dc.subjectProtein Binding
dc.subjectProtein Interaction Domains and Motifs
dc.subjectSequence Analysis, DNA
dc.subjectStructure-Activity Relationship
dc.titleStructural analysis of the woodland strawberry COI1-JAZ1 co-receptor for the plant hormone jasmonoyl-isoleucine
dc.typeArticle


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