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Fig. 4 | BMC Plant Biology

Fig. 4

From: Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites

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)

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