Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling
Glutathione peroxidases (GPXs) are non-heme peroxidases catalyzing the reduction of H<sub>2</sub>O<sub>2</sub> or organic hydroperoxides to water or corresponding alcohols using glutathione (GSH) or thioredoxin (TRX) as a reducing agent. In contrast to animal GPXs, the plant...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-08-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/11/8/1624 |
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| author | Krisztina Bela Riyazuddin Riyazuddin Jolán Csiszár |
| author_facet | Krisztina Bela Riyazuddin Riyazuddin Jolán Csiszár |
| author_sort | Krisztina Bela |
| collection | DOAJ |
| description | Glutathione peroxidases (GPXs) are non-heme peroxidases catalyzing the reduction of H<sub>2</sub>O<sub>2</sub> or organic hydroperoxides to water or corresponding alcohols using glutathione (GSH) or thioredoxin (TRX) as a reducing agent. In contrast to animal GPXs, the plant enzymes are non-seleno monomeric proteins that generally utilize TRX more effectively than GSH but can be a putative link between the two main redox systems. Because of the substantial differences compared to non-plant GPXs, use of the GPX-like (GPXL) name was suggested for <i>Arabidopsis</i> enzymes. GPX(L)s not only can protect cells from stress-induced oxidative damages but are crucial components of plant development and growth. Due to fine-tuning the H<sub>2</sub>O<sub>2</sub> metabolism and redox homeostasis, they are involved in the whole life cycle even under normal growth conditions. Significantly new mechanisms were discovered related to their transcriptional, post-transcriptional and post-translational modifications by describing gene regulatory networks, interacting microRNA families, or identifying Lys decrotonylation in enzyme activation. Their involvement in epigenetic mechanisms was evidenced. Detailed genetic, evolutionary, and bio-chemical characterization, and comparison of the main functions of GPXs, demonstrated their species-specific roles. The multisided involvement of GPX(L)s in the regulation of the entire plant life ensure that their significance will be more widely recognized and applied in the future. |
| first_indexed | 2024-03-09T10:02:54Z |
| format | Article |
| id | doaj.art-dec0d93c4f3848fdb2d03815271ee5aa |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-09T10:02:54Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-dec0d93c4f3848fdb2d03815271ee5aa2023-12-01T23:20:35ZengMDPI AGAntioxidants2076-39212022-08-01118162410.3390/antiox11081624Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and SignallingKrisztina Bela0Riyazuddin Riyazuddin1Jolán Csiszár2Department of Plant Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52., H-6726 Szeged, HungaryDepartment of Plant Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52., H-6726 Szeged, HungaryDepartment of Plant Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52., H-6726 Szeged, HungaryGlutathione peroxidases (GPXs) are non-heme peroxidases catalyzing the reduction of H<sub>2</sub>O<sub>2</sub> or organic hydroperoxides to water or corresponding alcohols using glutathione (GSH) or thioredoxin (TRX) as a reducing agent. In contrast to animal GPXs, the plant enzymes are non-seleno monomeric proteins that generally utilize TRX more effectively than GSH but can be a putative link between the two main redox systems. Because of the substantial differences compared to non-plant GPXs, use of the GPX-like (GPXL) name was suggested for <i>Arabidopsis</i> enzymes. GPX(L)s not only can protect cells from stress-induced oxidative damages but are crucial components of plant development and growth. Due to fine-tuning the H<sub>2</sub>O<sub>2</sub> metabolism and redox homeostasis, they are involved in the whole life cycle even under normal growth conditions. Significantly new mechanisms were discovered related to their transcriptional, post-transcriptional and post-translational modifications by describing gene regulatory networks, interacting microRNA families, or identifying Lys decrotonylation in enzyme activation. Their involvement in epigenetic mechanisms was evidenced. Detailed genetic, evolutionary, and bio-chemical characterization, and comparison of the main functions of GPXs, demonstrated their species-specific roles. The multisided involvement of GPX(L)s in the regulation of the entire plant life ensure that their significance will be more widely recognized and applied in the future.https://www.mdpi.com/2076-3921/11/8/1624antioxidantsglutathione peroxidasesgrowthreactive oxygen speciesredox statusstress responses |
| spellingShingle | Krisztina Bela Riyazuddin Riyazuddin Jolán Csiszár Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling Antioxidants antioxidants glutathione peroxidases growth reactive oxygen species redox status stress responses |
| title | Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling |
| title_full | Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling |
| title_fullStr | Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling |
| title_full_unstemmed | Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling |
| title_short | Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling |
| title_sort | plant glutathione peroxidases non heme peroxidases with large functional flexibility as a core component of ros processing mechanisms and signalling |
| topic | antioxidants glutathione peroxidases growth reactive oxygen species redox status stress responses |
| url | https://www.mdpi.com/2076-3921/11/8/1624 |
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