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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...

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Autores principales: Kotchoni, Simeon O., Jimenez-Lopez, Jose C., Gao, Dongying, Edwards, Vincent, Gachomo, Emma W., Margam, Venu M., Seufferheld, Manfredo J.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
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.
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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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