Insights on structure and function of a late embryogenesis abundant protein from Amaranthus cruentus: an intrinsically disordered protein involved in protection against desiccation, oxidant conditions, and osmotic stress

dc.creatorALMA LETICIA SAUCEDO YAÑEZ
dc.creatorERIC EDMUNDO HERNANDEZ DOMINGUEZ
dc.creatorLUIS ALBERTO DE LUNA VALDEZ
dc.creatorANGEL ARTURO GUEVARA GARCIA
dc.creatorABRAHAM ESCOBEDO MORATILLA
dc.creatorESAU BOJORQUEZ VELAZQUEZ
dc.creatorFederico del Rio Portilla
dc.creatorDANIEL ALEJANDRO FERNANDEZ VELASCO
dc.creatorANA PAULINA BARBA DE LA ROSA
dc.date2017-04
dc.date.accessioned2022-10-12T19:55:24Z
dc.date.available2022-10-12T19:55:24Z
dc.identifierhttp://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/1562
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4124939
dc.description"Late embryogenesis abundant (LEA) proteins are part of a large protein family that protect other proteins from aggregation due to desiccation or osmotic stresses. Recently, the Amaranthus cruentus seed proteome was characterized by 2D-PAGE and one highly accumulated protein spot was identified as a LEA protein and was named AcLEA. In this work, AcLEA cDNA was cloned into an expression vector and the recombinant protein was purified and characterized. AcLEA encodes a 172 amino acid polypeptide with a predicted molecular mass of 18.34 kDa and estimated pI of 8.58. Phylogenetic analysis revealed that AcLEA is evolutionarily close to the LEA3 group. Structural characteristics were revealed by nuclear magnetic resonance and circular dichroism methods. We have shown that recombinant AcLEA is an intrinsically disordered protein in solution even at high salinity and osmotic pressures, but it has a strong tendency to take a secondary structure, mainly folded as alpha-helix, when an inductive additive is present. Recombinant AcLEA function was evaluated using Escherichia coli as in vivo model showing the important protection role against desiccation, oxidant conditions, and osmotic stress. AcLEA recombinant protein was localized in cytoplasm of Nicotiana benthamiana protoplasts and orthologs were detected in seeds of wild and domesticated amaranth species. Interestingly AcLEA was detected in leaves, stems, and roots but only in plants subjected to salt stress. This fact could indicate the important role of AcLEA protection during plant stress in all amaranth species studied."
dc.formatapplication/pdf
dc.publisherFrontiers Media S.A
dc.relationinfo:eu-repo/semantics/altIdentifier/DOI/https://doi.org/10.3389/fpls.2017.00497
dc.relationcitation:Saucedo AL, Hernández-Domínguez EE, de Luna-Valdez LA, Guevara-García AA, Escobedo-Moratilla A, Bojorquéz-Velázquez E, del Río-Portilla F, Fernández-Velasco DA and Barba de la Rosa AP (2017) Insights on Structure and Function of a Late Embryogenesis Abundant Protein from Amaranthus cruentus: An Intrinsically Disordered Protein Involved in Protection against Desiccation, Oxidant Conditions, and Osmotic Stress. Front. Plant Sci. 8:497. doi: 10.3389/fpls.2017.00497
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0
dc.subjectinfo:eu-repo/classification/Autor/Amaranth seeds
dc.subjectinfo:eu-repo/classification/Autor/Circular dichroism
dc.subjectinfo:eu-repo/classification/Autor/Intrinsically disordered proteins (IDP)
dc.subjectinfo:eu-repo/classification/Autor/Late embryogenesis abundant (LEA) proteins
dc.subjectinfo:eu-repo/classification/Autor/Nuclear magnetic resonance
dc.subjectinfo:eu-repo/classification/Autor/Western blot
dc.subjectinfo:eu-repo/classification/cti/2
dc.subjectinfo:eu-repo/classification/cti/24
dc.subjectinfo:eu-repo/classification/cti/2415
dc.titleInsights on structure and function of a late embryogenesis abundant protein from Amaranthus cruentus: an intrinsically disordered protein involved in protection against desiccation, oxidant conditions, and osmotic stress
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion


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