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Molecular and structural insights into FaEXPA5, an alpha-expansin protein related with cell wall disassembly during ripening of strawberry fruit

dc.contributor.authorValenzuela-Riffo F.
dc.contributor.authorParra-Palma C.
dc.contributor.authorRamos P.
dc.contributor.authorMorales-Quintana L.
dc.date.accessioned2020-09-02T22:29:54Z
dc.date.available2020-09-02T22:29:54Z
dc.date.issued2020
dc.identifier10.1016/j.plaphy.2020.06.010
dc.identifier.citation154, , 581-589
dc.identifier.issn09819428
dc.identifier.urihttps://hdl.handle.net/20.500.12728/6509
dc.descriptionCell wall modification is one of the main factors that produce the tissue softening during ripening of many fruit including strawberry (Fragaria x ananassa). Expansins have been studied for over 20 years as a class of the important cell growth regulators, and in the last years these have been related with the fruit softening. In strawberry, five partial sequences of the expansins genes were described in the past, this analysis showed that FaEXP5 partial gene was present throughout fruit development, but was more strongly expressed during ripening. Now, we reported the full length of this α-expansin (FaEXPA5), whose had been related with fruit softening, and the protein structural was described by homology model. Their transcript accumulation during softening was confirmed by qRT-PCR, displaying a high accumulation rate during fruit ripening. In silico analysis of promoter sequence showed four ABA and two auxin cis-regulatory elements, potentially responsible for the expression patterns observed in response to the hormone treatments. Additionally, 3D protein model displayed two domains and one open groove characteristic of expansin structures. The protein–ligand interactions were evaluated by molecular dynamic (MD) simulation using three different long structure ligands (a cellulose fiber, a xyloglucan fiber (XXXG type), and a pectin fiber as control). Favorable interactions were observed with xyloglucan and cellulose, being cellulose the best ligand with lower RMSD value. Additionally, MD simulations showed that FaEXPA5 can interact with the ligands through residues present in the open groove along the two domains. © 2020 Elsevier Masson SAS
dc.language.isoen
dc.publisherElsevier Masson SAS
dc.subjectABA treatment
dc.subjectAlpha-expansins
dc.subjectAuxin treatment
dc.subjectFragaria ananassa
dc.subjectMolecular modeling
dc.titleMolecular and structural insights into FaEXPA5, an alpha-expansin protein related with cell wall disassembly during ripening of strawberry fruit
dc.typeArticle


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