Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity
Abstract Late Embryogenesis Abundant (LEA) proteins are a group of intrinsically disordered proteins implicated in plant responses to water deficit. In vitro studies revealed that LEA proteins protect reporter enzymes from inactivation during low water availability. Group 4 LEA proteins constitute a...
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| Format: | Article |
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Nature Portfolio
2024-02-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-024-53295-7 |
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| author | David F. Rendón-Luna Inti A. Arroyo-Mosso Haydee De Luna-Valenciano Francisco Campos Lorenzo Segovia Gloria Saab-Rincón Cesar L. Cuevas-Velazquez José Luis Reyes Alejandra A. Covarrubias |
| author_facet | David F. Rendón-Luna Inti A. Arroyo-Mosso Haydee De Luna-Valenciano Francisco Campos Lorenzo Segovia Gloria Saab-Rincón Cesar L. Cuevas-Velazquez José Luis Reyes Alejandra A. Covarrubias |
| author_sort | David F. Rendón-Luna |
| collection | DOAJ |
| description | Abstract Late Embryogenesis Abundant (LEA) proteins are a group of intrinsically disordered proteins implicated in plant responses to water deficit. In vitro studies revealed that LEA proteins protect reporter enzymes from inactivation during low water availability. Group 4 LEA proteins constitute a conserved protein family, displaying in vitro protective capabilities. Under water deficiency or macromolecular crowding, the N-terminal of these proteins adopts an alpha-helix conformation. This region has been identified as responsible for the protein in vitro protective activity. This study investigates whether the attainment of alpha-helix conformation and/or particular amino acid residues are required for the in vitro protective activity. The LEA4-5 protein from Arabidopsis thaliana was used to generate mutant proteins. The mutations altered conserved residues, deleted specific conserved regions, or introduced prolines to hinder alpha-helix formation. The results indicate that conserved residues are not essential for LEA4-5 protective function. Interestingly, the C-terminal region was found to contribute to this function. Moreover, alpha-helix conformation is necessary for the protective activity only when the C-terminal region is deleted. Overall, LEA4-5 shows the ability to adopt alternative functional conformations under the tested conditions. These findings shed light on the in vitro mechanisms by which LEA proteins protect against water deficit stress. |
| first_indexed | 2024-03-07T15:07:19Z |
| format | Article |
| id | doaj.art-7ce216e1b46a4bd2a20ef3ea120358dc |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-07T15:07:19Z |
| publishDate | 2024-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-7ce216e1b46a4bd2a20ef3ea120358dc2024-03-05T18:49:58ZengNature PortfolioScientific Reports2045-23222024-02-0114111310.1038/s41598-024-53295-7Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activityDavid F. Rendón-Luna0Inti A. Arroyo-Mosso1Haydee De Luna-Valenciano2Francisco Campos3Lorenzo Segovia4Gloria Saab-Rincón5Cesar L. Cuevas-Velazquez6José Luis Reyes7Alejandra A. Covarrubias8Departamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de MéxicoDepartamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoDepartamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoAbstract Late Embryogenesis Abundant (LEA) proteins are a group of intrinsically disordered proteins implicated in plant responses to water deficit. In vitro studies revealed that LEA proteins protect reporter enzymes from inactivation during low water availability. Group 4 LEA proteins constitute a conserved protein family, displaying in vitro protective capabilities. Under water deficiency or macromolecular crowding, the N-terminal of these proteins adopts an alpha-helix conformation. This region has been identified as responsible for the protein in vitro protective activity. This study investigates whether the attainment of alpha-helix conformation and/or particular amino acid residues are required for the in vitro protective activity. The LEA4-5 protein from Arabidopsis thaliana was used to generate mutant proteins. The mutations altered conserved residues, deleted specific conserved regions, or introduced prolines to hinder alpha-helix formation. The results indicate that conserved residues are not essential for LEA4-5 protective function. Interestingly, the C-terminal region was found to contribute to this function. Moreover, alpha-helix conformation is necessary for the protective activity only when the C-terminal region is deleted. Overall, LEA4-5 shows the ability to adopt alternative functional conformations under the tested conditions. These findings shed light on the in vitro mechanisms by which LEA proteins protect against water deficit stress.https://doi.org/10.1038/s41598-024-53295-7 |
| spellingShingle | David F. Rendón-Luna Inti A. Arroyo-Mosso Haydee De Luna-Valenciano Francisco Campos Lorenzo Segovia Gloria Saab-Rincón Cesar L. Cuevas-Velazquez José Luis Reyes Alejandra A. Covarrubias Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity Scientific Reports |
| title | Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity |
| title_full | Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity |
| title_fullStr | Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity |
| title_full_unstemmed | Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity |
| title_short | Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity |
| title_sort | alternative conformations of a group 4 late embryogenesis abundant protein associated to its in vitro protective activity |
| url | https://doi.org/10.1038/s41598-024-53295-7 |
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