title: Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure.
abstract: The phytotoxin coronatine is a structural analog of octadecanoid signaling molecules, which are well known mediators of plant defense reactions. To isolate novel coronatine-regulated genes from Arabidopsis thaliana, differential mRNA display was performed. Transcript levels of CORI-7 (coronatine induced-7) were rapidly and transiently increased in coronatine-treated plants, and the corresponding cDNA was found to encode the sulfotransferase AtST5a. Likewise, upon wounding, an immediate and transient increase in AtST5a mRNA levels could be observed in both locally wounded and unwounded (systemic) leaves. Furthermore, application of octadecanoids and ethylene as compounds involved in plant wound defense reactions resulted in AtST5a gene activation, whereas pathogen defense-related signals (yeast elicitor and salicylic acid) were inactive. AtST5a and its close homologs AtST5b and AtST5c were purified as His6-tagged proteins from Escherichia coli. The three enzymes were shown to catalyze the final step in the biosynthesis of the glucosinolate (GS) core structure, the sulfation of desulfoglucosinolates (dsGSs). They accept a broad range of dsGSs as substrates. However, in a competitive situation, AtST5a clearly prefers tryptophan- and phenylalanine-derived dsGSs, whereas long chain dsGSs derived from methionine are the preferred substrates of AtST5b and AtST5c. Treatment of Arabidopsis plants with low concentrations of coronatine resulted in an increase in the amounts of specific GSs, primarily glucobrassicin and neoglucobrassicin. Hence, it is suggested that AtST5a is the sulfotransferase responsible for the biosynthesis of tryptophan-derived GSs in vivo.
authors.affiliation: Department of Plant Physiology, Ruhr-Universität, Universitätsstrasse 150, 44801 Bochum, Germany.
authors.forename: Markus
authors.initials: M
authors.lastname: Piotrowski
authors.forename: Andreas
authors.initials: A
authors.lastname: Schemenewitz
authors.forename: Anna
authors.initials: A
authors.lastname: Lopukhina
authors.forename: Axel
authors.initials: A
authors.lastname: Müller
authors.forename: Tim
authors.initials: T
authors.lastname: Janowitz
authors.forename: Elmar W
authors.initials: EW
authors.lastname: Weiler
authors.forename: Claudia
authors.initials: C
authors.lastname: Oecking
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000096:biosynthesis / Q000737:chemistry; D001669:Biochemical Phenomena; D001671:Biochemistry; D015152:Blotting, Northern; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D005030:Ethylenes / Q000737:chemistry; D020869:Gene Expression Profiling; D018506:Gene Expression Regulation, Plant; D005961:Glucosinolates / Q000096:biosynthesis / Q000737:chemistry*; D007192:Indenes / Q000737:chemistry; D007211:Indoles / Q000737:chemistry; D008956:Models, Chemical; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013379:Substrate Specificity; D015238:Sulfotransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D013997:Time Factors; D015533:Transcriptional Activation; D014364:Tryptophan
chemical_list: D000596:Amino Acids; D029681:Arabidopsis Proteins; D018076:DNA, Complementary; D005030:Ethylenes; D005961:Glucosinolates; D007192:Indenes; D007211:Indoles; C058487:coronatine; D014364:Tryptophan; C036216:ethylene; C048308:glucobrassicin; C494865:CORI-7 protein, Arabidopsis; D015238:Sulfotransferases; C059883:desulfoglucosinolate sulfotransferase