Methyl transfer in glucosinolate biosynthesis mediated by indole glucosinolate O-Methyltransferase 5
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Methyl transfer in glucosinolate biosynthesis mediated by indole glucosinolate O-Methyltransferase 5. / Pfalz, Marina; Mukhaimar, Maisara; Perreau, François; Kirk, Jayne; Hansen, Cecilie Ida Cetti; Olsen, Carl Erik; Agerbirk, Niels; Kroymann, Juergen.
I: Plant Physiology, Bind 172, Nr. 4, 2016, s. 2190-2203.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Methyl transfer in glucosinolate biosynthesis mediated by indole glucosinolate O-Methyltransferase 5
AU - Pfalz, Marina
AU - Mukhaimar, Maisara
AU - Perreau, François
AU - Kirk, Jayne
AU - Hansen, Cecilie Ida Cetti
AU - Olsen, Carl Erik
AU - Agerbirk, Niels
AU - Kroymann, Juergen
N1 - © 2016 American Society of Plant Biologists. All Rights Reserved.
PY - 2016
Y1 - 2016
N2 - Indole glucosinolates (IGs) are plant secondary metabolites that are derived from the amino acid tryptophan. The product of Arabidopsis (Arabidopsis thaliana) IG core biosynthesis, indol-3-ylmethyl glucosinolate (I3M), can be modified by hydroxylation and subsequent methoxylation of the indole ring in position 1 (1-IG modification) or 4 (4-IG modification). Products of the 4-IG modification pathway mediate plant-enemy interactions and are particularly important for Arabidopsis innate immunity. While CYP81Fs encoding cytochrome P450 monooxygenases and IGMTs encoding indole glucosinolate O-methyltransferases have been identified as key genes for IG modification, our knowledge about the IG modification pathways is not complete. In particular, it is unknown which enzyme is responsible for methyl transfer in the 1-IG modification pathway and whether this pathway plays a role in defense, similar to 4-IG modification. Here, we analyze two Arabidopsis transfer DNA insertion lines with targeted metabolomics. We show that biosynthesis of 1-methoxyindol-3-ylmethyl glucosinolate (1MOI3M) from I3M involves the predicted unstable intermediate 1-hydroxyindol-3-ylmethyl glucosinolate (1OHI3M) and that IGMT5, a gene with moderate similarity to previously characterized IGMTs, encodes the methyltransferase that is responsible for the conversion of 1OHI3M to 1MOI3M. Disruption of IGMT5 function increases resistance against the root-knot nematode Meloidogyne javanica and suggests a potential role for the 1-IG modification pathway in Arabidopsis belowground defense.
AB - Indole glucosinolates (IGs) are plant secondary metabolites that are derived from the amino acid tryptophan. The product of Arabidopsis (Arabidopsis thaliana) IG core biosynthesis, indol-3-ylmethyl glucosinolate (I3M), can be modified by hydroxylation and subsequent methoxylation of the indole ring in position 1 (1-IG modification) or 4 (4-IG modification). Products of the 4-IG modification pathway mediate plant-enemy interactions and are particularly important for Arabidopsis innate immunity. While CYP81Fs encoding cytochrome P450 monooxygenases and IGMTs encoding indole glucosinolate O-methyltransferases have been identified as key genes for IG modification, our knowledge about the IG modification pathways is not complete. In particular, it is unknown which enzyme is responsible for methyl transfer in the 1-IG modification pathway and whether this pathway plays a role in defense, similar to 4-IG modification. Here, we analyze two Arabidopsis transfer DNA insertion lines with targeted metabolomics. We show that biosynthesis of 1-methoxyindol-3-ylmethyl glucosinolate (1MOI3M) from I3M involves the predicted unstable intermediate 1-hydroxyindol-3-ylmethyl glucosinolate (1OHI3M) and that IGMT5, a gene with moderate similarity to previously characterized IGMTs, encodes the methyltransferase that is responsible for the conversion of 1OHI3M to 1MOI3M. Disruption of IGMT5 function increases resistance against the root-knot nematode Meloidogyne javanica and suggests a potential role for the 1-IG modification pathway in Arabidopsis belowground defense.
U2 - 10.1104/pp.16.01402
DO - 10.1104/pp.16.01402
M3 - Journal article
C2 - 27810943
VL - 172
SP - 2190
EP - 2203
JO - Plant Physiology
JF - Plant Physiology
SN - 0032-0889
IS - 4
ER -
ID: 169991162