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. 2021 Jul 5;21:322. doi: 10.1186/s12870-021-03087-2

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© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data.

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Fig. 2 — Overview of evolution of plastid glutathione-related redox networks in land plants and streptophyte algae. Schematic overview of the plastid GSH-dependent redox network in land plant model species and the streptophyte alga C. braunii. Electrons from photosynthetic electron transport (PET) contribute to ROS generation and at the same time to ROS scavenging, damage repair and redox homeostasis. H₂O₂ leads to lipid peroxidation (L-O-O-H) as well as oxidation of protein methionine (Met-R-SO), of ascorbic acid (AsA) to dehydroascorbate (DHA) or protein thiol oxidation to the respective sulfenic acid (RS-OH) that can react with GSH to form an S-glutathionylated adduct (RS-SG). Glutaredoxins (GRX) can (de) glutathionylate proteins. The balance between the reduced tripeptide glutathione (GSH) and glutathione disulfide (GSSG) is influenced by GSSG generation via enzymes involved in ROS/RNS scavenging or protein as well as lipid repair, such as dehydroascorbate reductase (DHAR), atypical (1 Cys) methionine sulfoxide reductases B1 (MSRB1), lambda and iota-type (?, function not confirmed in vitro) glutathione S-transferases and type II peroxiredoxins (PRX). Glutathione reductase (GR, NADPH-dependent) safeguards a highly reduced GSH-pool. The presence of at least one plastid-targeted isoform of a protein in a model species (assessed by presence of an N-terminal extension and targeting predictions, see Additional files 1, 2, 3, 4, 5, 6, 7, 8) is represented by a coloured box in the species legend next to the protein. A coloured box with question mark means the potential presence of an isoform as targeting prediction is unclear, but N-terminal extension indicating a targeting peptide is present (see Additional files 1, 2, 3, 4, 5, 6, 7, 8). Absence of a box can either mean absence of homologs from that species (see Fig. 1), or that all homologs do not have N-terminal extensions or that gene models are fragmentary (see Additional files 1, 2, 3, 4, 5, 6, 7, 8). Species legend: Chara braunii (Cb), Anthoceros agrestis (Aa), Marchantia polymorpha (Mp), Physcomitrium patens (Pp), Selaginella moellendorffii (Sm), Salvinia cucullata (Sc), Azolla filiculoides (Af), Brachypodium distachyon (Bd) and Arabidopsis thaliana (At)