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Fig. 6 in Comparison of glucosinolate diversity in the crucifer tribe Cardamineae and the remaining order Brassicales highlights repetitive evolutionary loss and gain of biosynthetic steps

Fig. 6. Aspects of glucosinolate (GSL) evolution in the order Brassicales with focus on the tribe Cardamineae. A. Phylogeny matched with GSL structural or biosynthetic features. Structural and biochemical features of GSL profiles of the respective species are indicated as deduced precursor amino acids and deduced modification of parent GSLs from the various precursors. Categories are based on GSL profiles as in Fig. 5C, but interpreted in a biosynthetic context. Presence of para- hydroxylated phenyl groups can potentially be due to either use of a specific precursor amino acid (Tyr or homoTyr) or a specific modification (para-hydroxylation), and is hence shown in an intermediate position, with the relevant backbones shown in B. Panel C shows the deduced modification steps. For the phylogeny in A, phylogenetic relationships based on Bayesian inference (MrBayes) of ITS regions were calculated for a subset of species from Brassicaceae and using Reseda (Resedaceae) as outgroup. Labels for B. vulgaris (group 3, group 7) refer to the ITS sequence pools listed in Agerbirk et al., (in review). Bootstrap values from 1000 replicates are shown for Bayesian and maximum-likelihood inference, respectively. Side-chain modification exclusively known from n-homoMet derived GSLs (Fig. 5B) is left out for space-considerations. For GSL profile data, group 7 of B. vulgaris was assumed to represent ssp. vulgaris.

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Fig. 5 in Comparison of glucosinolate diversity in the crucifer tribe Cardamineae and the remaining order Brassicales highlights repetitive evolutionary loss and gain of biosynthetic steps

Fig. 5. Structural redundancy and innovation in glucosinolate (GSL) biodiversity. A. Representative GSL structures categorized as ancient due to presence in nonBrassicaceae members of the order Brassicales. The poorly known status for a substituted Trp-derived is indicated (see text). B. Representative GSLs from three derived families (Capparaceae, Cleomaceae and Brassicaceae) with a simplified indication of the biosynthetic connections of n-homoMet derived GSLs. C. Distribution of three groups of GSLs in selected members of the tribes Cardamineae, Arabideae and Brassiceae. The first group, those illustrated in panel A, seem to be due to ancient or recapitulated biosynthesis. The second group seem to be of intermediate age, the n-homoMet derived are pooled for space considerations. Possibly, the 4-substituted Trp derived 4moIM (48) and homoIle derived 54 and 29 also belongs to this group. The third group is deduced to represent recently evolved biosyntheses, as discussed in text, and the GSLs are illustrated in panel D. The category "Present" in panel C indicates one or more conclusive demonstrations of the relevant GSL, while "Tested, not reported" means that relevant organs have been tested using relevant methods, yet the GSL was not reported, although explicit search for the GSL was not necessarily reported. Hence we could not conclude the GSL to be "not found", although this would be the simplest interpretation. The category "Circumstantial evidence" means that reasonable but not conclusive evidence for the relevant GSL has been published, while the category "Insufficent or missing data" means that relevant organs (roots for substituted Trp-derived and seeds for SGlc-acylated) have not been sufficiently investigated using methods with demonstrated ability to reveal the GSL in question.

Fig. 6 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 6. Diversification of CYP81F enzymes in the Camelineae species.A neighbor-joining tree of CYP81F proteins from the investigated species. AtCYP83B1 was used as an outgroup. The bar represents 10% sequence divergence.

Fig. 3 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 3. Expression of genes encoding glucosinolate biosynthetic enzymes correlates with product accumulation. Relative expression levels of selected genes encoding enzymes involved in the core glucosinolate biosynthesis were determined by RT-qPCR method using gene encoding actin as a reference. The obtained values were normalized by dividing each of them by the maximal value obtained for the tested gene in the respective species. Results are means ± SD from three independent experiments, each with four biological replicates (n = 12).

Fig. 1 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 1. General scheme of aliphatic and indolic glucosinolate biosynthesis. Dashed arrows represent multistage processes. GLs – glucosinolates, I3G – 3- indolylmethyl GL, 1OHI3G – 1-hydroxy-I3G, 4OHI3G – 4-hydroxy-I3G, 1MI3G – 1-methoxy-I3G, 4MI3G – 4-methoxy-I3G.

Fig. 5 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 5. Divergence of the CYP81F1/3/4 locus in the Camelineae species.Graphical representation of genomic regions containing putative CYP81F1, CYP81F3 and CYP81F4 orthologs in selected Brassicaceae plants. Roman numbers indicate chromosome numbers (if available). Gene orientations are indicated by arrows.

Fig. 8 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 8. IGMT phylogenetic tree is incongruent with the phylogeny of the investigated species. A neighbor-joining phylogenetic tree of IGMT proteins from the investigated species. A. thaliana O-methyltransferase 1 (AtOMT1) was used as an outgroup. The bar represents 10% sequence divergence.

Fig. 7 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 7. Divergence of the IGMT1-4 locus in the Camelineae species. Graphical representation of genomic regions containing putative IGMT1-4 orthologs in selected Brassicaceae plants. Roman numbers indicate chromosome numbers (if available). Gene orientation are indicated by arrows.

Fig. 2 in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 2. Total accumulation of glucosinolates varies strongly between particular organs and between investigated species. Bar graphs indicate total peak areas of AG and IG molecular ions obtained during LC/MS analysis. The results and are means ± SD from three independent experiments with three biological replicates in each (n = 9). Significantly different statistical groups indicated by ANOVA (P <0.05, Tukey's test) are shown with upper-case (AGs) and lowercase (IGs) letters. AGs – aliphatic glucosinolates, IGs – indolic glucosinolates; # - not detected

Fig. 4. The investigated Camelineae species differ from A in Evolutionary changes in the glucosinolate biosynthetic capacity in species representing Capsella, Camelina and Neslia genera

Fig. 4. The investigated Camelineae species differ from A. thaliana in their glucosinolate modification capacity. Bar graphs indicate peak areas of particular molecular ions corresponding to methylsulfinylalkyl-aliphatic glucosinolates (AGs) and to indolic glucosinolates (IGs) detected during LC/MS analysis in siliques, inflorescences and roots of mature plants. The obtained values are means ± SD from three independent experiments with three biological replicates in each (n = 9). MeSO – methylsulfinylalkyl, GL – glucosinolate, I3G – 3-indolylmethyl GL, 1MI3G – 1-methoxy-I3G, 4OHI3G – 4-hydroxy-I3G, 4MI3G – 4-methoxy-I3G, # - not detected

Fig. 28 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 28. The desulfation reaction catalyzed by sulfatase and used for derivatization in glucosinolate analysis.

Fig. 26 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 26. Mixed reaction catalyzed by "nitrilase" enzymes in crucifers. (A) The strict functional definition of nitrilase activity (E.C. 3.5.5.1). (B) A side reaction catalyzed by crucifer nitrilases to variable degree, probably caused by premature termination of the reaction after the first round of addition of water (Jandhyala et al., 2005), functionally defined as nitrile hydratase activity (E.C. 4.2.1.84).

Fig. 24 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 24. Examples of glucosinolate-derived indole phytoalexins and biosynthetic connections. Asterisks indicate a selected example of a labeling study of the brassinin biosynthesis (Pedras and Yaya, 2013). Question marks above some arrows signify steps that are demonstrated in vivo but for which specific enzymes are not yet known. MYR, myrosinase.

Fig. 25 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 25. Examples of crucifer non-indole phytoalexins derived from phenethyl isothiocyanate (Pedras and To, 2018). Question marks above some arrows signify steps that are demonstrated in vivo but for which specific enzymes are not yet known. MYR, myrosinase.

Fig. 22 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 22. Diverse products of allyl glucosinolate (GSL) depending on presence or absence of specifier proteins. The asterisks over the GSL, the isothiocyanate and the thiocyanate summarize the results of labeling studies (Benn, 1977; Rossiter et al., 2007) as previously detailed (Agerbirk and Olsen, 2012). All GSLs can form isothiocyanates, although some may be unstable, and nitriles. Only aliphatic GSLs with a terminal unsaturation can form epithionitriles. Only allyl GSL and two other GSLs (formally able to form a resonance-stabilized cation) can form organic thiocyanates. Some specifier proteins have other activities than those they are named from, as indicated in brackets. MYR, myrosinase; ESP, epithiospecifier protein; NSP, nitrile specifier protein; TFP, thiocyanate-forming protein.

Fig. 23 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 23. Participation of glutathione and a glutathione-S-transferase in forming a GSL-derived amine as a product of glucosinolate metabolism in intact cells, important for plant immunity. Question marks above some arrows signify steps that are demonstrated in vivo but for which specific enzymes are not yet known. Reactions are unbalanced. Amine and acid products are illustrated as the corresponding ammonium and carboxylate ions, as they would mainly exist at physiological pH. MYR, myrosinase.

Fig. 21 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 21. Selected examples of glucosinolate analogs synthesized for studying the interaction of natural glucosinolates with myrosinase.

Fig. 20 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 20. Synthesis of a glucosinolate epitope coupled to bovine serum albumin (BSA), intended for elicitation of an immune response.

Fig. 17 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 17. Two novel glucosinolates demonstrated by NMR and MS, but without conclusion of a single structure since the position of the methyl group is undetermined in each case.

Fig. 29 in Glucosinolate structural diversity, identification, chemical synthesis and metabolism in plants

Fig. 29. Possible sites for formation of isomers of the constant part of glucosinolates. Very high numbers of isomers of glucosinolates suggested in two recent publications could potentially be such "isoglucosinolates".