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SOT17 (gene locus At1g18590) encodes a cytosolic sulfotransferase in Arabidopsis thaliana, also designated as AtSOT17, AtST5c, or ST5C in the literature (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7, hirschmann2014themultiproteinfamily pages 3-4). The protein belongs to the sulfotransferase 1 family and contains the characteristic P-loop NTPase and sulfotransferase domains consistent with its enzymatic function (hirschmann2017characterizationofdesulfoglucosinolate pages 28-60, hirschmann2014themultiproteinfamily pages 2-3).
SOT17 (At1g18590; AtST5c) is a cytoplasmic, PAPS-dependent desulfoglucosinolate sulfotransferase that catalyzes the terminal step of glucosinolate core biosynthesis. It transfers a sulfate group from 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to a desulfoglucosinolate, generating PAP and the corresponding mature glucosinolate; this sulfation completes the glucosinolate core structure. SOT17 acts alongside the related SOT16 and SOT18 enzymes but is functionally differentiated by its preference for long-chain, methionine-derived desulfoglucosinolates—particularly C6–C8 substrates—while lacking detectable activity toward tryptophan-derived indolic substrates. Available evidence places this soluble enzyme and its reaction in the cytoplasm, although protein-specific microscopy evidence is limited. (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7, hirschmann2017characterizationofdesulfoglucosinolate pages 28-60, hirschmann2014themultiproteinfamily pages 2-3, hirschmann2014themultiproteinfamily pages 7-8, hirschmann2017characterizationofdesulfoglucosinolate pages 13-18)
Blockquote: SOT17 completes glucosinolate core biosynthesis by sulfating selected desulfoglucosinolate precursors in the cytoplasm. Its distinct substrate preferences differentiate it from the related SOT16 and SOT18 enzymes.
SOT17 catalyzes the final step in the biosynthesis of the glucosinolate core structure by transferring a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to desulfoglucosinolates (dsGSs), producing mature glucosinolates and 3'-phosphoadenosine 5'-phosphate (PAP) as products (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7, hirschmann2017characterizationofdesulfoglucosinolate pages 13-18). This PAPS-dependent sulfation reaction completes the assembly of the glucosinolate core structure, which consists of a β-thioglucose moiety, a sulfonated aldoxime group, and a variable amino acid-derived side chain (hirschmann2014themultiproteinfamily pages 6-7, qin2023developingmultifunctionalcrops pages 4-5).
SOT17 exhibits relatively narrow substrate specificity compared to its paralog SOT16 (hirschmann2014themultiproteinfamily pages 7-8). Biochemical characterization using recombinant enzyme demonstrated that SOT17's preferred substrate is 8-methylthiooctyl desulfoglucosinolate (8MTO-dsGS), a long-chain, methionine-derived aliphatic glucosinolate precursor (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7). The enzyme accepts a range of desulfoglucosinolate substrates with varying efficiencies:
| Enzyme | Preferred substrates | Substrate classes | Key distinguishing features |
|---|---|---|---|
| AtSOT16 (AtST5a) | Tryptophan-derived and phenylalanine-derived desulfoglucosinolates; also accepts methionine-derived C3–C8 substrates at lower activity | Indolic: preferred; aromatic: preferred; aliphatic: accepted | Broadest substrate spectrum of the three enzymes; strongly associated with indole-glucosinolate biosynthesis and can sulfate multiple precursor classes. (hirschmann2014themultiproteinfamily pages 3-4, hirschmann2014themultiproteinfamily pages 7-8, hirschmann2017characterizationofdesulfoglucosinolate pages 70-74) |
| AtSOT17 (AtST5c) | Long-chain, methionine-derived desulfoglucosinolates, especially C6–C8; also accepts benzyl desulfoglucosinolate | Aliphatic: preferred, especially long-chain; aromatic: accepted; indolic: no detected activity | Most active in the reported assay toward 8-methylthiooctyl desulfoglucosinolate; more selective than SOT16 and favors long-chain aliphatic precursors. (hirschmann2014themultiproteinfamily pages 7-8, piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
| AtSOT18 (AtST5b) | Methionine-derived desulfoglucosinolates, particularly long-chain methylthioalkyl substrates such as C7 and C8 precursors | Aliphatic: preferred; aromatic: some activity reported; indolic: little or no activity | Overlaps with SOT17 in long-chain aliphatic specificity but is distinct in substrate and PAPS affinity; substrate preferences can vary among Arabidopsis ecotypes. (hirschmann2014themultiproteinfamily pages 3-4, hirschmann2017characterizationofdesulfoglucosinolate pages 60-65, hirschmann2014themultiproteinfamily pages 7-8, hirschmann2017characterizationofdesulfoglucosinolate pages 70-74) |
Table: Comparison of the three Arabidopsis desulfoglucosinolate sulfotransferases by precursor class and preferred substrates. The table highlights SOT17’s defining preference for long-chain methionine-derived precursors and lack of detectable indolic activity.
The enzyme shows a marked preference for long-chain methionine-derived substrates with C6, C7, and C8 side chains, while exhibiting substantially lower activity toward shorter-chain (C4) or S-oxygenated derivatives (hirschmann2014themultiproteinfamily pages 7-8). Importantly, SOT17 does not act on tryptophan-derived indolic desulfoglucosinolates, distinguishing it from the related enzyme SOT16, which preferentially sulfates indolic and aromatic substrates (hirschmann2014themultiproteinfamily pages 7-8, hirschmann2017characterizationofdesulfoglucosinolate pages 70-74).
| Substrate | Substrate class | Relative activity or preference | Key citations |
|---|---|---|---|
| 8-Methylthiooctyl desulfoglucosinolate (8MTO-dsGS; C8) | Aliphatic; methionine-derived, long-chain | 100%; preferred substrate | (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7, hirschmann2017characterizationofdesulfoglucosinolate pages 60-65) |
| 7-Methylthioheptyl desulfoglucosinolate (C7) | Aliphatic; methionine-derived, long-chain | 58% | (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7, hirschmann2017characterizationofdesulfoglucosinolate pages 60-65) |
| Benzyl desulfoglucosinolate | Aromatic; phenylalanine-derived | 30%; accepted aromatic substrate | (hirschmann2014themultiproteinfamily pages 7-8, piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
| 3-Butenyl desulfoglucosinolate | Aliphatic; methionine-derived | 27% | (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
| 4-Methylthiobutyl desulfoglucosinolate (C4) | Aliphatic; methionine-derived | 19% | (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
| 8-Methylsulfinyloctyl desulfoglucosinolate (C8) | Aliphatic; methionine-derived, long-chain and S-oxygenated | 8% | (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
| 4-Methylsulfinylbutyl desulfoglucosinolate (C4) | Aliphatic; methionine-derived and S-oxygenated | 3% | (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
| Tryptophan-derived desulfoglucosinolates | Indolic | No detectable activity reported | (hirschmann2014themultiproteinfamily pages 7-8) |
| Overall specificity | Primarily aliphatic, with some aromatic activity | Favors methionine-derived substrates with long C6–C8 side chains; 8MTO-dsGS is the strongest tested substrate | (hirschmann2014themultiproteinfamily pages 7-8, piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7) |
Table: Relative activities are normalized to SOT17/AtST5c activity toward 8MTO-dsGS. The profile demonstrates a preference for long-chain methionine-derived desulfoglucosinolates, limited aromatic activity, and no reported activity toward indolic substrates.
This substrate specificity has been confirmed through both in vitro enzyme assays using purified recombinant protein and analysis of glucosinolate profiles in Arabidopsis plants (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 6-7, piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 3-4).
SOT17 is a cytoplasmic, soluble sulfotransferase that carries out its function in the cytosolic compartment (hirschmann2017characterizationofdesulfoglucosinolate pages 28-60, hirschmann2014themultiproteinfamily pages 2-3). The protein lacks membrane-targeting sequences or organellar localization signals and can be purified from the soluble cellular fraction (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 3-4). This cytoplasmic localization is consistent with the overall organization of the glucosinolate biosynthesis pathway, where the core structure assembly occurs predominantly in the cytosol, although some early side-chain elongation reactions take place in chloroplasts (bogahawatta2023knockoutoftranscription pages 15-19).
Glucosinolate biosynthesis proceeds through three major stages: (1) amino acid side-chain modification and elongation, (2) core structure formation, and (3) secondary modifications (qin2023developingmultifunctionalcrops pages 4-5, kitainda2024molecularmechanismsbehind pages 20-25). SOT17 functions at the terminal step of core structure formation, after the following upstream reactions have occurred:
For methionine-derived aliphatic glucosinolates, the precursor amino acid undergoes iterative chain elongation through the action of methylthioalkylmalate synthase (MAMS), isopropylmalate isomerase (IPMI), and isopropylmalate dehydrogenase (IPMDH) in chloroplasts, followed by transamination by branched-chain aminotransferases (BCATs) (kitainda2024molecularmechanismsbehind pages 16-20, kitainda2024molecularmechanismsbehind pages 29-33). The elongated amino acids or their corresponding oxo-acids are then converted to aldoximes by CYP79 enzymes, which are subsequently oxidized by CYP83 enzymes (qin2023developingmultifunctionalcrops pages 4-5, kitainda2024molecularmechanismsbehind pages 20-25). Glutathione-S-transferases conjugate glutathione to these intermediates, and the C-S lyase SUR1 generates thiohydroximic acids (kitainda2024molecularmechanismsbehind pages 20-25, kitainda2024molecularmechanismsbehind pages 39-44). UDP-glucosyltransferases UGT74B1 and UGT74C1 then add glucose to produce desulfoglucosinolates (qin2023developingmultifunctionalcrops pages 4-5, kitainda2024molecularmechanismsbehind pages 20-25).
At this point, SOT17, along with its paralogs SOT16 and SOT18, catalyzes the sulfation of these desulfoglucosinolate intermediates to generate the mature glucosinolate core structure (hirschmann2017characterizationofdesulfoglucosinolate pages 13-18, hirschmann2014themultiproteinfamily pages 8-9, hirschmann2017characterizationofdesulfoglucosinolate pages 28-60). Following core formation, the glucosinolates may undergo further secondary modifications including S-oxygenation by flavin monooxygenases (FMOGS-OX enzymes), side-chain alterations by AOP2/AOP3 enzymes, and other modifications that generate structural diversity (qin2023developingmultifunctionalcrops pages 4-5, kitainda2024molecularmechanismsbehind pages 20-25).
Arabidopsis possesses three desulfoglucosinolate sulfotransferases—SOT16, SOT17, and SOT18—that together ensure sulfation of the diverse array of desulfoglucosinolate substrates produced by the plant (hirschmann2014themultiproteinfamily pages 3-4, hirschmann2017characterizationofdesulfoglucosinolate pages 28-60). These enzymes share at least 72% amino acid sequence identity yet exhibit distinct catalytic preferences (hirschmann2017characterizationofdesulfoglucosinolate pages 28-60):
This functional differentiation allows the plant to efficiently sulfate the full range of desulfoglucosinolate precursors and likely contributes to the varied glucosinolate profiles observed across different tissues, developmental stages, and environmental conditions (hirschmann2014themultiproteinfamily pages 6-7).
Glucosinolates are nitrogen- and sulfur-containing specialized metabolites that function primarily as chemical defense compounds in Brassicaceae plants (hirschmann2014themultiproteinfamily pages 6-7, piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 1-1). In their intact form, glucosinolates are stable, non-toxic compounds stored in plant cells (bogahawatta2023knockoutoftranscription pages 15-19). Their defensive function is activated upon tissue damage by herbivores or pathogens: physical disruption brings glucosinolates into contact with myrosinase enzymes (thioglucosidases), which are normally compartmentalized in separate myrosin cells (hirschmann2014themultiproteinfamily pages 6-7, bogahawatta2023knockoutoftranscription pages 15-19).
Myrosinase-mediated hydrolysis cleaves the glucose moiety, releasing an unstable aglycone that spontaneously rearranges to form biologically active products including isothiocyanates, thiocyanates, nitriles, epithionitriles, and oxazolidine-2-thiones (hirschmann2014themultiproteinfamily pages 6-7, kitainda2024molecularmechanismsbehind pages 16-20, piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 1-1). The specific products formed depend on the glucosinolate side-chain structure, pH, temperature, and the presence of cofactors or additional proteins such as epithiospecifier proteins (bogahawatta2023knockoutoftranscription pages 15-19, kitainda2024molecularmechanismsbehind pages 16-20). These breakdown products exhibit toxicity or deterrent effects against herbivorous insects, fungal pathogens, and bacteria, thereby protecting the plant (kitainda2024molecularmechanismsbehind pages 16-20, kitainda2024molecularmechanismsbehind pages 8-16, he2026comparativegenomicsand pages 1-2).
Glucosinolates and their breakdown products also have significance for human nutrition and health, with isothiocyanates showing potential anticancer properties, although some products can also have goitrogenic or antinutritional effects (piotrowski2004desulfoglucosinolatesulfotransferasesfrom pages 1-1, kitainda2024molecularmechanismsbehind pages 8-16, choi2026abi5mediatedabasignaling pages 1-4).
SOT17 is constitutively expressed across major aerial tissues including leaves, flowers, and siliques (hirschmann2014themultiproteinfamily pages 7-8). However, its expression is strongly developmentally regulated, with the highest transcript levels observed in two-week-old seedlings and the lowest levels in flowering plants (hirschmann2014themultiproteinfamily pages 7-8, hirschmann2014themultiproteinfamily pages 8-9). This developmental pattern suggests that SOT17-mediated glucosinolate biosynthesis is particularly important during the early seedling stage, when defense compound accumulation may be critical for survival (hirschmann2014themultiproteinfamily pages 7-8).
SOT17 expression responds to multiple environmental and hormonal signals:
Light regulation: SOT17 transcript levels exhibit diurnal regulation under a 12-hour light/12-hour dark cycle, with expression peaking at the end of the light period and reaching minimum levels at the end of the dark period (hirschmann2014themultiproteinfamily pages 8-9). This light-dependent regulation is consistent with the coordinated control of glucosinolate biosynthesis genes (hirschmann2014themultiproteinfamily pages 8-9).
Jasmonate signaling: SOT17 expression is significantly induced by jasmonate treatment, consistent with a role in defense responses (hirschmann2014themultiproteinfamily pages 8-9, hirschmann2014themultiproteinfamily pages 7-8). Coronatine, a bacterial virulence signal that mimics jasmonate, produces only a modest (~1.3-fold) increase in SOT17 expression, suggesting some specificity in the hormonal response (hirschmann2014themultiproteinfamily pages 8-9, hirschmann2014themultiproteinfamily pages 7-8).
Stress responses: In the related species Eutrema salsugineum, the SOT17 ortholog is strongly upregulated by UV irradiation and silver nitrate (AgNO₃) treatment, suggesting involvement in stress-induced defense metabolism (mucha2015substantialreprogrammingof pages 8-9).
The regulation of SOT17 expression reflects its integration into defensive and adaptive metabolic programs that respond to environmental challenges (xiong2025quantitativetraitloci pages 15-17).
Recent studies have continued to explore the role of desulfoglucosinolate sulfotransferases in Brassicaceae crops and their relatives. A 2024 study on natural variation in sulfur content among Arabidopsis accessions found that SOT17 and SOT18 expression levels were significantly elevated in high-sulfur accessions, suggesting these enzymes contribute to the connection between sulfur homeostasis and glucosinolate biosynthesis (jager2024traitslinkedto pages 1-2). Targeted proteomics approaches developed in 2024 have enabled quantification of SOT17 protein levels alongside transcripts and metabolites in glucosinolate pathway studies, revealing that SOT17 protein is below detection limits in jasmonate signaling mutants (myc2/3/4), consistent with its jasmonate-responsive expression (vik2024standardflowtargetedproteomics pages 2-3).
A 2025 study on indole-3-carbinol content in Brassica napus emphasized the conserved role of SOT genes including SOT17 orthologs in the final sulfation step of glucosinolate biosynthesis across Brassicaceae species (xiong2025quantitativetraitloci pages 15-17). These recent findings underscore the continued relevance of SOT17 and related enzymes in crop quality, nutritional value, and stress tolerance.
SOT17 is a specialized cytoplasmic sulfotransferase that catalyzes the PAPS-dependent sulfation of desulfoglucosinolates, completing the final step in glucosinolate core biosynthesis. Its preference for long-chain methionine-derived aliphatic substrates, particularly 8-methylthiooctyl desulfoglucosinolate, distinguishes it from the related SOT16 (which favors indolic substrates) and SOT18 enzymes. SOT17 functions in the cytosol as part of the glucosinolate biosynthesis pathway, which produces specialized metabolites essential for plant defense against herbivores and pathogens. The enzyme's expression is regulated by developmental stage, light conditions, and jasmonate signaling, integrating glucosinolate biosynthesis with growth, circadian rhythms, and defense responses. Through its specific substrate preferences and coordinated regulation, SOT17 contributes to the diversity and tissue-specific patterns of glucosinolate accumulation in Arabidopsis thaliana.
References
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