TY - JOUR
T1 - Molecular basis of the evolution of methylthioalkylmalate synthase and the diversity of methionine-derived glucosinolates
AU - Kumar, Roshan
AU - Lee, Soon Goo
AU - Augustine, Rehna
AU - Reichelt, Micheal
AU - Vassão, Daniel G.
AU - Palavalli, Manoj H.
AU - Allen, Aron
AU - Gershenzon, Jonathan
AU - Jez, Joseph M.
AU - Bisht, Naveen C.
N1 - Funding Information:
We thank the Central Instrumentation and Plant Growth Facilities at the National Institute for Plant Genome Research (NIPGR). Portions of this research were carried out at the Argonne National Laboratory Structural Biology Center of the Advanced Photon Source, a national use facility operated by the University of Chicago for the U.S. Department of Energy Office of Biological and Environmental Research (grant DE-AC02-06CH11357). The work was supported by the Department of Biotechnology, Ministry of Science and Technology, India (grants BT/PR271/AGR/36/ 687/2011 and BT/06/IYBA/2012 to N.C.B.); the National Science Foundation (grant NSF-MCB-1614539 to J.M.J.), and a grant from the Max Planck Society to J.G. Support was also provided by a NIPGR Short Term Overseas Fellowship to N.C.B.; by a Max Planck India Fellowship to N.C.B.; by the University Grants Commission (India) to R.K.; and by NIPGR to R.A.
Funding Information:
We thank the Central Instrumentation and Plant Growth Facilities at the National Institute for Plant Genome Research (NIPGR). Portions of this research were carried out at the Argonne National Laboratory Structural Biology Center of the Advanced Photon Source, a national use facility operated by the University of Chicago for the U.S. Department of Energy Office of Biological and Environmental Research (grant DE-AC02- 06CH11357). The work was supported by the Department of Biotechnology, Ministry of Science and Technology, India (grants BT/PR271/AGR/36/687/2011 and BT/06/IYBA/2012 to N.C.B.); the National Science Foundation (grant NSF-MCB-1614539 to J.M.J.), and a grant from the Max Planck Society to J.G. Support was also provided by a NIPGR Short Term Overseas Fellowship to N.C.B.; by aMaxPlanck India Fellowship to N.C.B.; by the University Grants Commission (India) to R.K.; and by NIPGR to R.A.
Publisher Copyright:
© 2019 ASPB.
PY - 2019/7
Y1 - 2019/7
N2 - The globally cultivated Brassica species possess diverse aliphatic glucosinolates, which are important for plant defense and animal nutrition. The committed step in the side chain elongation of methionine-derived aliphatic glucosinolates is catalyzed by methylthioalkylmalate synthase, which likely evolved from the isopropylmalate synthases of leucine biosynthesis. However, the molecular basis for the evolution of methylthioalkylmalate synthase and its generation of natural product diversity in Brassica is poorly understood. Here, we show that Brassica genomes encode multiple methylthioalkylmalate synthases that have differences in expression profiles and 2-oxo substrate preferences, which account for the diversity of aliphatic glucosinolates across Brassica accessions. Analysis of the 2.1 Å resolution x-ray crystal structure of Brassica juncea methylthioalkylmalate synthase identified key active site residues responsible for controlling the specificity for different 2-oxo substrates and the determinants of side chain length in aliphatic glucosinolates. Overall, these results provide the evolutionary and biochemical foundation for the diversification of glucosinolate profiles across globally cultivated Brassica species, which could be used with ongoing breeding strategies toward the manipulation of beneficial glucosinolate compounds for animal health and plant protection.
AB - The globally cultivated Brassica species possess diverse aliphatic glucosinolates, which are important for plant defense and animal nutrition. The committed step in the side chain elongation of methionine-derived aliphatic glucosinolates is catalyzed by methylthioalkylmalate synthase, which likely evolved from the isopropylmalate synthases of leucine biosynthesis. However, the molecular basis for the evolution of methylthioalkylmalate synthase and its generation of natural product diversity in Brassica is poorly understood. Here, we show that Brassica genomes encode multiple methylthioalkylmalate synthases that have differences in expression profiles and 2-oxo substrate preferences, which account for the diversity of aliphatic glucosinolates across Brassica accessions. Analysis of the 2.1 Å resolution x-ray crystal structure of Brassica juncea methylthioalkylmalate synthase identified key active site residues responsible for controlling the specificity for different 2-oxo substrates and the determinants of side chain length in aliphatic glucosinolates. Overall, these results provide the evolutionary and biochemical foundation for the diversification of glucosinolate profiles across globally cultivated Brassica species, which could be used with ongoing breeding strategies toward the manipulation of beneficial glucosinolate compounds for animal health and plant protection.
UR - http://www.scopus.com/inward/record.url?scp=85069622262&partnerID=8YFLogxK
U2 - 10.1105/tpc.19.00046
DO - 10.1105/tpc.19.00046
M3 - Article
C2 - 31023839
AN - SCOPUS:85069622262
SN - 1040-4651
VL - 31
SP - 1633
EP - 1647
JO - Plant Cell
JF - Plant Cell
IS - 7
ER -