Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes

Monodehydroascorbate reductase (MDAR) is an enzyme involved in ascorbate recycling. <i>Arabidopsis thaliana</i> has five <i>MDAR</i> genes that encode two cytosolic, one cytosolic/peroxisomal, one peroxisomal membrane-attached, and one chloroplastic/mitochondrial isoform. In...

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Autores principales: Mio Tanaka, Ryuki Takahashi, Akane Hamada, Yusuke Terai, Takahisa Ogawa, Yoshihiro Sawa, Takahiro Ishikawa, Takanori Maruta
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Publicado: MDPI AG 2021
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spelling oai:doaj.org-article:2425bec247c0408dae49fa228278c9412021-11-25T16:27:17ZDistribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes10.3390/antiox101117262076-3921https://doaj.org/article/2425bec247c0408dae49fa228278c9412021-10-01T00:00:00Zhttps://www.mdpi.com/2076-3921/10/11/1726https://doaj.org/toc/2076-3921Monodehydroascorbate reductase (MDAR) is an enzyme involved in ascorbate recycling. <i>Arabidopsis thaliana</i> has five <i>MDAR</i> genes that encode two cytosolic, one cytosolic/peroxisomal, one peroxisomal membrane-attached, and one chloroplastic/mitochondrial isoform. In contrast, tomato plants possess only three enzymes, lacking the cytosol-specific enzymes. Thus, the number and distribution of MDAR isoforms differ according to plant species. Moreover, the physiological significance of MDARs remains poorly understood. In this study, we classify plant MDARs into three classes: class I, chloroplastic/mitochondrial enzymes; class II, peroxisomal membrane-attached enzymes; and class III, cytosolic/peroxisomal enzymes. The cytosol-specific isoforms form a subclass of class III and are conserved only in Brassicaceae plants. With some exceptions, all land plants and a charophyte algae, <i>Klebsormidium flaccidum</i>, contain all three classes. Using reverse genetic analysis of <i>Arabidopsis thaliana</i> mutants lacking one or more isoforms, we provide new insight into the roles of MDARs; for example, (1) the lack of two isoforms in a specific combination results in lethality, and (2) the role of MDARs in ascorbate redox regulation in leaves can be largely compensated by other systems. Based on these findings, we discuss the distribution and function of MDAR isoforms in land plants and their cooperation with other recycling systems.Mio TanakaRyuki TakahashiAkane HamadaYusuke TeraiTakahisa OgawaYoshihiro SawaTakahiro IshikawaTakanori MarutaMDPI AGarticleascorbate recyclingmonodehydroascorbate reductasedehydroascorbate reductaselight stress<i>Arabidopsis thaliana</i>Therapeutics. PharmacologyRM1-950ENAntioxidants, Vol 10, Iss 1726, p 1726 (2021)
institution DOAJ
collection DOAJ
language EN
topic ascorbate recycling
monodehydroascorbate reductase
dehydroascorbate reductase
light stress
<i>Arabidopsis thaliana</i>
Therapeutics. Pharmacology
RM1-950
spellingShingle ascorbate recycling
monodehydroascorbate reductase
dehydroascorbate reductase
light stress
<i>Arabidopsis thaliana</i>
Therapeutics. Pharmacology
RM1-950
Mio Tanaka
Ryuki Takahashi
Akane Hamada
Yusuke Terai
Takahisa Ogawa
Yoshihiro Sawa
Takahiro Ishikawa
Takanori Maruta
Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes
description Monodehydroascorbate reductase (MDAR) is an enzyme involved in ascorbate recycling. <i>Arabidopsis thaliana</i> has five <i>MDAR</i> genes that encode two cytosolic, one cytosolic/peroxisomal, one peroxisomal membrane-attached, and one chloroplastic/mitochondrial isoform. In contrast, tomato plants possess only three enzymes, lacking the cytosol-specific enzymes. Thus, the number and distribution of MDAR isoforms differ according to plant species. Moreover, the physiological significance of MDARs remains poorly understood. In this study, we classify plant MDARs into three classes: class I, chloroplastic/mitochondrial enzymes; class II, peroxisomal membrane-attached enzymes; and class III, cytosolic/peroxisomal enzymes. The cytosol-specific isoforms form a subclass of class III and are conserved only in Brassicaceae plants. With some exceptions, all land plants and a charophyte algae, <i>Klebsormidium flaccidum</i>, contain all three classes. Using reverse genetic analysis of <i>Arabidopsis thaliana</i> mutants lacking one or more isoforms, we provide new insight into the roles of MDARs; for example, (1) the lack of two isoforms in a specific combination results in lethality, and (2) the role of MDARs in ascorbate redox regulation in leaves can be largely compensated by other systems. Based on these findings, we discuss the distribution and function of MDAR isoforms in land plants and their cooperation with other recycling systems.
format article
author Mio Tanaka
Ryuki Takahashi
Akane Hamada
Yusuke Terai
Takahisa Ogawa
Yoshihiro Sawa
Takahiro Ishikawa
Takanori Maruta
author_facet Mio Tanaka
Ryuki Takahashi
Akane Hamada
Yusuke Terai
Takahisa Ogawa
Yoshihiro Sawa
Takahiro Ishikawa
Takanori Maruta
author_sort Mio Tanaka
title Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes
title_short Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes
title_full Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes
title_fullStr Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes
title_full_unstemmed Distribution and Functions of Monodehydroascorbate Reductases in Plants: Comprehensive Reverse Genetic Analysis of <i>Arabidopsis thaliana</i> Enzymes
title_sort distribution and functions of monodehydroascorbate reductases in plants: comprehensive reverse genetic analysis of <i>arabidopsis thaliana</i> enzymes
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/2425bec247c0408dae49fa228278c941
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