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Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features
The completion of the rice genome sequence has made it possible to identify and characterize new genes and to perform comparative genomics studies across taxa. The aldehyde dehydrogenase (ALDH) gene superfamily encoding for NAD(P)(+)-dependent enzymes is found in all major plant and animal taxa. How...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2902511/ https://www.ncbi.nlm.nih.gov/pubmed/20634950 http://dx.doi.org/10.1371/journal.pone.0011516 |
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author | Kotchoni, Simeon O. Jimenez-Lopez, Jose C. Gao, Dongying Edwards, Vincent Gachomo, Emma W. Margam, Venu M. Seufferheld, Manfredo J. |
author_facet | Kotchoni, Simeon O. Jimenez-Lopez, Jose C. Gao, Dongying Edwards, Vincent Gachomo, Emma W. Margam, Venu M. Seufferheld, Manfredo J. |
author_sort | Kotchoni, Simeon O. |
collection | PubMed |
description | The completion of the rice genome sequence has made it possible to identify and characterize new genes and to perform comparative genomics studies across taxa. The aldehyde dehydrogenase (ALDH) gene superfamily encoding for NAD(P)(+)-dependent enzymes is found in all major plant and animal taxa. However, the characterization of plant ALDHs has lagged behind their animal- and prokaryotic-ALDH homologs. In plants, ALDHs are involved in abiotic stress tolerance, male sterility restoration, embryo development and seed viability and maturation. However, there is still no structural property-dependent functional characterization of ALDH protein superfamily in plants. In this paper, we identify members of the rice ALDH gene superfamily and use the evolutionary nesting events of retrotransposons and protein-modeling–based structural reconstitution to report the genetic and molecular and structural features of each member of the rice ALDH superfamily in abiotic/biotic stress responses and developmental processes. Our results indicate that rice-ALDHs are the most expanded plant ALDHs ever characterized. This work represents the first report of specific structural features mediating functionality of the whole families of ALDHs in an organism ever characterized. |
format | Text |
id | pubmed-2902511 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-29025112010-07-15 Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features Kotchoni, Simeon O. Jimenez-Lopez, Jose C. Gao, Dongying Edwards, Vincent Gachomo, Emma W. Margam, Venu M. Seufferheld, Manfredo J. PLoS One Research Article The completion of the rice genome sequence has made it possible to identify and characterize new genes and to perform comparative genomics studies across taxa. The aldehyde dehydrogenase (ALDH) gene superfamily encoding for NAD(P)(+)-dependent enzymes is found in all major plant and animal taxa. However, the characterization of plant ALDHs has lagged behind their animal- and prokaryotic-ALDH homologs. In plants, ALDHs are involved in abiotic stress tolerance, male sterility restoration, embryo development and seed viability and maturation. However, there is still no structural property-dependent functional characterization of ALDH protein superfamily in plants. In this paper, we identify members of the rice ALDH gene superfamily and use the evolutionary nesting events of retrotransposons and protein-modeling–based structural reconstitution to report the genetic and molecular and structural features of each member of the rice ALDH superfamily in abiotic/biotic stress responses and developmental processes. Our results indicate that rice-ALDHs are the most expanded plant ALDHs ever characterized. This work represents the first report of specific structural features mediating functionality of the whole families of ALDHs in an organism ever characterized. Public Library of Science 2010-07-12 /pmc/articles/PMC2902511/ /pubmed/20634950 http://dx.doi.org/10.1371/journal.pone.0011516 Text en Kotchoni et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Kotchoni, Simeon O. Jimenez-Lopez, Jose C. Gao, Dongying Edwards, Vincent Gachomo, Emma W. Margam, Venu M. Seufferheld, Manfredo J. Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features |
title | Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features |
title_full | Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features |
title_fullStr | Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features |
title_full_unstemmed | Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features |
title_short | Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features |
title_sort | modeling-dependent protein characterization of the rice aldehyde dehydrogenase (aldh) superfamily reveals distinct functional and structural features |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2902511/ https://www.ncbi.nlm.nih.gov/pubmed/20634950 http://dx.doi.org/10.1371/journal.pone.0011516 |
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