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PMID: 11706188 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway.

Plant physiology ·Vol. 127 ·No. 3 ·2001-11-00 ·Pages 1077-88

Kroymann J, Textor S, Tokuhisa JG, Falk KL, Bartram S, Gershenzon J, Mitchell-Olds T

Abstract

Arabidopsis and other Brassicaceae produce an enormous diversity of aliphatic glucosinolates, a group of methionine (Met)-derived plant secondary compounds containing a beta-thio-glucose moiety, a sulfonated oxime, and a variable side chain. We fine-scale mapped GSL-ELONG, a locus controlling variation in the side-chain length of aliphatic glucosinolates. Within this locus, a polymorphic gene was identified that determines whether Met is extended predominantly by either one or by two methylene groups to produce aliphatic glucosinolates with either three- or four-carbon side chains. Two allelic mutants deficient in four-carbon side-chain glucosinolates were shown to contain independent missense mutations within this gene. In cell-free enzyme assays, a heterologously expressed cDNA from this locus was capable of condensing 2-oxo-4-methylthiobutanoic acid with acetyl-coenzyme A, the initial reaction in Met chain elongation. The gene methylthioalkylmalate synthase1 (MAM1) is a member of a gene family sharing approximately 60% amino acid sequence similarity with 2-isopropylmalate synthase, an enzyme of leucine biosynthesis that condenses 2-oxo-3-methylbutanoate with acetyl-coenzyme A.

MeSH Terms
2-Isopropylmalate Synthase/metabolism Acetyl Coenzyme A/metabolism Arabidopsis/genetics,metabolism Chromosome Mapping Exons Gene Expression Regulation, Plant Glucosinolates/genetics,metabolism Introns Methionine/metabolism Molecular Sequence Data Multigene Family Oxo-Acid-Lyases/genetics Peptide Chain Elongation, Translational
Chemicals
Glucosinolates Acetyl Coenzyme A Methionine 2-Isopropylmalate Synthase Oxo-Acid-Lyases methylthioalkylmalate synthase 1
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Kroymann J
Department of Genetics and Evolution, Max Planck Institute for Chemical Ecology, Carl-Zeiss-Promenade 10, 07745 Jena, Germany.
Textor S
Tokuhisa J G
Falk K L
Bartram S
Gershenzon J
Mitchell-Olds T
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Article Info
Journal
Plant physiology
Abbr.
Plant Physiol
ISSN
0032-0889
Published
2001-11-00
Pages
1077-88
Language
English
Region
United States
NLM ID
0401224
PMCID
PMC129277
Subset
IM
Databases
GENBANK
AB006708, AB026660, AC013354, AC016662, AF004165, AF004166
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