dc.date.accessioned2019-05-16T13:40:16Z
dc.date.accessioned2022-10-18T22:23:05Z
dc.date.available2019-05-16T13:40:16Z
dc.date.available2022-10-18T22:23:05Z
dc.date.created2019-05-16T13:40:16Z
dc.date.issued2018
dc.identifierhttp://hdl.handle.net/10533/235676
dc.identifier1140663
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4467031
dc.description.abstractThe phytohormone jasmonates (JAs) regulate fundamental plant processes; such 30 as the anthocyanin accumulation during ripening of strawberry, a non-climacteric fruit model. 31 Jasmonoyl-isoleucine (JA-Ile), one of the bioactive JA molecules, mediates binding of the JAZ 32 repressor protein to COI1, an F-box protein forming the SCFCOI1 ubiquitin E3 ligase complex, in 33 Arabidopsis. The COI1-JA-Ile-JAZ complex initiates the JA-signaling pathway leading to early 34 jasmonate responses. Most of Arabidopsis JAZs contain a degron sequence at the Jas domain 35 responsible for interaction with COI1 and JA-Ile. The woodland strawberry (Fragaria vesca) is a 36 model plant for the Rosaceae family, in which the JA-signaling pathway is poorly understood at 37 the molecular level. The aim of this work was to understand the molecular basis of the 38 interaction between the F. vesca COI1 (FvCOI1) and JAZ1 (FvJAZ1) or JAZ8 (FvJAZ8) 39 mediated by JA-Ile. 40 Methods. Multiple alignments of amino acid sequences and phylogenetic analyses were 41 performed for FvCOI1 and FvJAZ1/8 and their ortholog sequences. The FvCOI1 and FvJAZ1/8 42 3D structures were built by homology modeling methods, which were further refined and 43 validated by molecular dynamics simulation (MDS). A molecular docking approach along with 44 MDS analysis were used to understand the interaction capacity between a putative degron-like 45 present in FvJAZ1 and FvJAZ8 with the FvCOI1-JA-Ile and FvCOI1-JA complexes. 46 Results. FvCOI1 and FvJAZ1/8 showed high and moderate identity, respectively, with the 47 corresponding ortholog proteins from other plant species including apple, grape, tomato and 48 Arabidopsis. The resulting FvCOI1 structural model showed that the F-box and LRR domains 49 were highly similar to that described in Arabidopsis COI1 (AtCOI1) crystal structure. 50 Unexpectedly, we found that FvJAZ1 has a variant IPMQRK sequence respect to the canonical 51 LPIAR(R/K) degron sequence observed in AtJAZ1. The MDS results showed that the FvCOI1- 52 JA-Ile-FvJAZ1 complex was the most stable among all the analyzed ones, and the IPMQRK 53 peptide of FvJAZ1 interacted directly with FvCOI1 and JA-Ile. In contrast, FvJAZ8 did not show 54 a direct interaction with those two components, as expected from previous experimental results 55 for the ortholog AtJAZ8. 56 Discussion. The present research provides novel insight into the molecular interactions between 57 key JA-signaling components in the model plant F. vesca. Remarkably, we characterized the PeerJ Preprints | https://doi.org/10.7287/peerj.preprints.2772v2 | CC BY 4.0 Open Access | rec: 14 Jan 2018, publ: 14 Jan 2018 3 IPMQRK sequence present in FvJAZ1, a putative variant 58 of the canonical degron previously 59 described in AtJAZ1. We propose that the FvCOI1-JA-Ile-FvJAZ1 complex is stable, and that 60 the degron-like sequence present in FvJAZ1 interacts in a steady manner with FvCOI1-JA-Ile. 61 Up to now, this is the first structural characterization of molecular interactions that may be 62 occurring between the core components of the JA-Ile perception complex in a fleshy fruit-related 63 species.
dc.languageeng
dc.relationinfo:eu-repo/grantAgreement//1140663
dc.relationinfo:eu-repo/semantics/dataset/hdl.handle.net/10533/93482
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI2.0
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.titleStructural characterization 1 of the jasmonoyl-isoleucine 2 perception complexes from Fragaria vesca by in silico 3 molecular analysis
dc.typeManuscrito


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