Show simple item record

Title

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.contributor.authorSaucedo Yáñez, Alma Leticia
dc.contributor.authorHernández Domínguez, Eric Edmundo
dc.contributor.authorDe Luna Valdez, Luis Alberto
dc.contributor.authorGuevara Garcia, Angel Arturo
dc.contributor.authorEscobedo-Moratilla, Abraham
dc.contributor.authorBojórquez Velázquez, Esaú
dc.contributor.authorDel Rio Portilla, Federico
dc.contributor.authorFernández Velasco, Daniel Alejandro
dc.contributor.authorBarba de la Rosa, Ana Paulina
dc.date.accessioned2018-07-11T18:29:32Z
dc.date.available2018-07-11T18:29:32Z
dc.date.issued2017-05
dc.identifier.citationSaucedo 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.identifier.urihttp://hdl.handle.net/11627/4000
dc.description.abstract"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.publisherFrontiers Media S.A.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectAmaranth seeds
dc.subjectCircular dichroism
dc.subjectIntrinsically disordered proteins (IDP)
dc.subjectLate embryogenesis abundant (LEA) proteins
dc.subjectNuclear magnetic resonance
dc.subjectWestern blot
dc.subject.classificationBIOLOGÍA MOLECULAR
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.typearticle
dc.identifier.doihttps://doi.org/10.3389/fpls.2017.00497
dc.rights.accessAcceso Abierto


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 Internacional