Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/91671
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Type: Journal article
Title: New insights into the evolutionary history of plant sorbitol dehydrogenase
Author: Jia, Y.
Wong, D.
Sweetman, C.
Bruning, J.
Ford, C.
Citation: BMC Plant Biology, 2015; 15(1):101-1-101-23
Publisher: BioMed Central
Issue Date: 2015
ISSN: 1471-2229
1471-2229
Statement of
Responsibility: 
Yong Jia, Darren CJ Wong, Crystal Sweetman, John B Bruning and Christopher M Ford
Abstract: Background: Sorbitol dehydrogenase (SDH, EC 1.1.1.14) is the key enzyme involved in sorbitol metabolism in higher plants. SDH genes in some Rosaceae species could be divided into two groups. L-idonate-5-dehydrogenase (LIDH, EC 1.1.1.264) is involved in tartaric acid (TA) synthesis in Vitis vinifera and is highly homologous to plant SDHs. Despite efforts to understand the biological functions of plant SDH, the evolutionary history of plant SDH genes and their phylogenetic relationship with the V. vinifera LIDH gene have not been characterized. Results: A total of 92 SDH genes were identified from 42 angiosperm species. SDH genes have been highly duplicated within the Rosaceae family while monocot, Brassicaceae and most Asterid species exhibit singleton SDH genes. Core Eudicot SDHs have diverged into two phylogenetic lineages, now classified as SDH Class I and SDH Class II. V. vinifera LIDH was identified as a Class II SDH. Tandem duplication played a dominant role in the expansion of plant SDH family and Class II SDH genes were positioned in tandem with Class I SDH genes in several plant genomes. Protein modelling analyses of V. vinifera SDHs revealed 19 putative active site residues, three of which exhibited amino acid substitutions between Class I and Class II SDHs and were influenced by positive natural selection in the SDH Class II lineage. Gene expression analyses also demonstrated a clear transcriptional divergence between Class I and Class II SDH genes in V. vinifera and Citrus sinensis (orange. Conclusions: Phylogenetic, natural selection and synteny analyses provided strong support for the emergence of SDH Class II by positive natural selection after tandem duplication in the common ancestor of core Eudicot plants. The substitutions of three putative active site residues might be responsible for the unique enzyme activity of V. vinifera LIDH, which belongs to SDH Class II and represents a novel function of SDH in V. vinifera that may be true also of other Class II SDHs. Gene expression analyses also supported the divergence of SDH Class II at the expression level. This study will facilitate future research into understanding the biological functions of plant SDHs.
Keywords: Sorbitol dehydrogenase; L-idonate-5-dehydrogenase; Gene duplication; Functional divergence; Tartaric acid; Ascorbic acid; Grapevine
Description: Published online: 12 April 2015
Rights: © 2015 Jia et al.; licensee BioMed Central. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
RMID: 0030027681
DOI: 10.1186/s12870-015-0478-5
Appears in Collections:Agriculture, Food and Wine publications

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