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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. 4 — Evolutionary conservation of known S-glutathionylation sites on non-catalytic cysteines. Schematic representation of five target proteins with non-conserved and non-catalytic cysteines showing interesting patterns of evolutionary conservation regarding S-glutathionylation sites (see Additional file 10 for alignments). To generate the alignments BlastP results were filtered manually by clades based on phylogenetic trees and additionally length of the N-terminus and TargetP [45, 46] predictions to identify the organellar isoforms of phosphoglycerate kinase (a), alpha-amylase (AMY3) (b), thiamine thiazole synthase (THI1) (c), apoferredoxin (FDX) (d) and 3’phosphoadenosine 5′ phosphate phosphatase (SAL1) (e). The bars indicate the total length of the proteins and are aligned with the position of the glutathionylated cysteine. In the case of two cysteine positions, the proteins were aligned to the cysteine that is conserved in more species. Gaps in the alignments are not indicated in this graph. The known glutathionylated cysteine sites are marked with a red square in the respective organism. Asterisks indicate putative cytosolic isoforms (TargetP [45, 46] predictions) regarding PGK. Synechocystis sp. (WP), Chara braunii (Chbra), Anthoceros agrestis (Aa), Marchantia polymorpha (Mapoly), Physcomitrium patens (Pp), Selaginella moellendorffii (Selmo), Salvinia cucullata (Sacu), Azolla filiculoides (Azfi), Brachypodium distachyon (Bradi) and Arabidopsis thaliana (At)