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http://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/1562| 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 | |
| ALMA LETICIA SAUCEDO YAÑEZ ERIC EDMUNDO HERNANDEZ DOMINGUEZ LUIS ALBERTO DE LUNA VALDEZ ANGEL ARTURO GUEVARA GARCIA ABRAHAM ESCOBEDO MORATILLA ESAU BOJORQUEZ VELAZQUEZ Federico del Rio Portilla DANIEL ALEJANDRO FERNANDEZ VELASCO ANA PAULINA BARBA DE LA ROSA | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.3389/fpls.2017.00497 | |
| Amaranth seeds Circular dichroism Intrinsically disordered proteins (IDP) Late embryogenesis abundant (LEA) proteins Nuclear magnetic resonance Western blot | |
| "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." | |
| Frontiers Media S.A | |
| 2017-04 | |
| Artículo | |
| 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 | |
| BIOLOGÍA MOLECULAR | |
| Versión publicada | |
| publishedVersion - Versión publicada | |
| Aparece en las colecciones: | Publicaciones Científicas Biología Molecular |
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