Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis

Malate dehydrogenase (MDH, EC 1.1.1.37) is a key enzyme that catalyzes a reversible NAD-dependent dehydrogenase reaction from oxaloacetate (OAA) to malate. Although MDH has been documented to participate in cellular metabolism and redox homeostasis in plants, the roles of MDH members in the tropical...

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Main Authors: Song, Jianling, Zou Xiaoyan, Liu, Pandao, Cardoso Arango, Juan Andrés, Schultze-Kraft, Rainer, Liu, Guodao, Luo, Lijuan, Chen, Zhijian
Format: Journal Article
Language:Inglés
Published: Elsevier 2022
Subjects:
Online Access:https://hdl.handle.net/10568/117447
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author Song, Jianling
Zou Xiaoyan
Liu, Pandao
Cardoso Arango, Juan Andrés
Schultze-Kraft, Rainer
Liu, Guodao
Luo, Lijuan
Chen, Zhijian
author_browse Cardoso Arango, Juan Andrés
Chen, Zhijian
Liu, Guodao
Liu, Pandao
Luo, Lijuan
Schultze-Kraft, Rainer
Song, Jianling
Zou Xiaoyan
author_facet Song, Jianling
Zou Xiaoyan
Liu, Pandao
Cardoso Arango, Juan Andrés
Schultze-Kraft, Rainer
Liu, Guodao
Luo, Lijuan
Chen, Zhijian
author_sort Song, Jianling
collection Repository of Agricultural Research Outputs (CGSpace)
description Malate dehydrogenase (MDH, EC 1.1.1.37) is a key enzyme that catalyzes a reversible NAD-dependent dehydrogenase reaction from oxaloacetate (OAA) to malate. Although MDH has been documented to participate in cellular metabolism and redox homeostasis in plants, the roles of MDH members in the tropical legume Stylosanthes guianensis (stylo) remain less definitive. In this study, except SgMDH1 that had been previously characterized, six novel MDH genes were isolated from stylo and were then designated as SgMDH2 to SgMDH7. All of the SgMDH proteins possessed the common features of NAD binding, dimerization interface and substrate binding sites. Expression analysis showed that three SgMDHs exhibited preferential expressions in leaves, and one SgMDH was mainly expressed in roots. Furthermore, SgMDHs were regulated by nutrient deficiencies in stylo roots, especially for phosphorus (-P) and potassium (-K) deficiencies. Differential responses of SgMDHs to trace metal stress and heavy metal toxicity were observed in stylo roots, suggesting the involvement of SgMDHs in the response of stylo to metal stresses. The six novel SgMDHs were subsequently expressed and purified from Escherichia coli to analyze their biochemical properties. Although SgMDHs exhibited variations in subcellular localizations, each SgMDH protein displayed a high level of catalytic efficiency towards OAA and NADH but a low level of catalytic efficiency towards malate and NAD+. In addition, the activities of recombinant SgMDH proteins were pH-dependent and temperature-sensitive, and exhibited differential regulations by various metal ions. These results together suggest the potential roles of SgMDHs in stylo coping with nutrient and metal stresses.
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spelling CGSpace1174472025-11-11T18:51:36Z Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis Song, Jianling Zou Xiaoyan Liu, Pandao Cardoso Arango, Juan Andrés Schultze-Kraft, Rainer Liu, Guodao Luo, Lijuan Chen, Zhijian gene expression nutrient deficiencies malate dehydrogenase enzymes properties stylosanthes guianensis expresión génica deficiencias nutritivas malato deshidrogenasa Malate dehydrogenase (MDH, EC 1.1.1.37) is a key enzyme that catalyzes a reversible NAD-dependent dehydrogenase reaction from oxaloacetate (OAA) to malate. Although MDH has been documented to participate in cellular metabolism and redox homeostasis in plants, the roles of MDH members in the tropical legume Stylosanthes guianensis (stylo) remain less definitive. In this study, except SgMDH1 that had been previously characterized, six novel MDH genes were isolated from stylo and were then designated as SgMDH2 to SgMDH7. All of the SgMDH proteins possessed the common features of NAD binding, dimerization interface and substrate binding sites. Expression analysis showed that three SgMDHs exhibited preferential expressions in leaves, and one SgMDH was mainly expressed in roots. Furthermore, SgMDHs were regulated by nutrient deficiencies in stylo roots, especially for phosphorus (-P) and potassium (-K) deficiencies. Differential responses of SgMDHs to trace metal stress and heavy metal toxicity were observed in stylo roots, suggesting the involvement of SgMDHs in the response of stylo to metal stresses. The six novel SgMDHs were subsequently expressed and purified from Escherichia coli to analyze their biochemical properties. Although SgMDHs exhibited variations in subcellular localizations, each SgMDH protein displayed a high level of catalytic efficiency towards OAA and NADH but a low level of catalytic efficiency towards malate and NAD+. In addition, the activities of recombinant SgMDH proteins were pH-dependent and temperature-sensitive, and exhibited differential regulations by various metal ions. These results together suggest the potential roles of SgMDHs in stylo coping with nutrient and metal stresses. 2022-01 2022-01-11T14:11:33Z 2022-01-11T14:11:33Z Journal Article https://hdl.handle.net/10568/117447 en Limited Access application/pdf Elsevier Song, J.; Zou, X.; Liu, P.; Cardoso, J.A.; Schultze-Kraft, R.; Liu, G.; Luo, L.; Chen, Z., (2022) Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis. Plant Physiology and Biochemistry 170 p. 325-337. ISSN: 0981-9428
spellingShingle gene expression
nutrient deficiencies
malate dehydrogenase
enzymes
properties
stylosanthes guianensis
expresión génica
deficiencias nutritivas
malato deshidrogenasa
Song, Jianling
Zou Xiaoyan
Liu, Pandao
Cardoso Arango, Juan Andrés
Schultze-Kraft, Rainer
Liu, Guodao
Luo, Lijuan
Chen, Zhijian
Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis
title Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis
title_full Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis
title_fullStr Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis
title_full_unstemmed Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis
title_short Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis
title_sort differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in stylosanthes guianensis
topic gene expression
nutrient deficiencies
malate dehydrogenase
enzymes
properties
stylosanthes guianensis
expresión génica
deficiencias nutritivas
malato deshidrogenasa
url https://hdl.handle.net/10568/117447
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