TY - JOUR
T1 - Genomics and biochemical analyses reveal a metabolon key to β-L-ODAP biosynthesis in Lathyrus sativus
AU - Edwards, Anne
AU - Njaci, Isaac
AU - Sarkar, Abhimanyu
AU - Jiang, Zhouqian
AU - Kaithakottil, Gemy George
AU - Moore, Christopher
AU - Cheema, Jitender
AU - Stevenson, Clare E. M.
AU - Rejzek, Martin
AU - Novák, Petr
AU - Vigouroux, Marielle
AU - Vickers, Martin
AU - Wouters, Roland H. M.
AU - Paajanen, Pirita
AU - Steuernagel, Burkhard
AU - Moore, Jonathan D.
AU - Higgins, Janet
AU - Swarbreck, David
AU - Martens, Stefan
AU - Kim, Colin Y.
AU - Weng, Jing-Ke
AU - Mundree, Sagadevan
AU - Kilian, Benjamin
AU - Kumar, Shiv
AU - Loose, Matt
AU - Yant, Levi
AU - Macas, Jiří
AU - Wang, Trevor L.
AU - Martin, Cathie
AU - Emmrich, Peter
N1 - Data availability statement: LS007 genomic PromethION and Illumina sequencing data generated in this study have been deposited in the European Nucleotide Archive under accession PRJEB33571. Illumina RNAseq and HiC raw data generated in this study have been deposited in the NCBI Gene Expression Omnibus under accession GSE223956. The genome assembly and annotations generated in this study have been deposited on Zenodo [https://zenodo.org/record/7390878]. All plant materials used in this article are available from the corresponding author. Source data are provided with this paper.
Funding information: This work was supported by a John Innes Centre Institute Development Grant awarded to C.M., the Biotechnology and Biological Sciences Research Council (BBSRC) Detox Grass pea project (BB/L011719/1) awarded to C.M. and T.L.W., the BBSRC SASSA UPGRADE project (BB/R020604/1) awarded to C.M. and S.K., the BBSRC Institute Strategic Programmes ‘Understanding and Exploiting Plant and Microbial Secondary Metabolism’ (BB/J004596/1) and ‘Molecules from Nature’ (BB/P012523/1) which supported C.M., T.L.W., B.S. and the Nottingham Future Food Beacon of Excellence supporting L.Y. and M.L. and the Templeton World Charity Foundation, Inc. (TWCF0400), awarded to C.M., S.K. and B.K. P.M.F.E.’s studentship was funded by the John Innes Foundation’s Student Rotation programme. None of the funding bodies were involved in the design of this study, the collection or analysis or interpretation of data, or in writing the manuscript.
PY - 2023/2/16
Y1 - 2023/2/16
N2 - Grass pea (Lathyrus sativus L.) is a rich source of protein cultivated as an insurance crop in Ethiopia, Eritrea, India, Bangladesh, and Nepal. Its resilience to both drought and flooding makes it a promising crop for ensuring food security in a changing climate. The lack of genetic resources and the crop’s association with the disease neurolathyrism have limited the cultivation of grass pea. Here, we present an annotated, long read-based assembly of the 6.5 Gbp L. sativus genome. Using this genome sequence, we have elucidated the biosynthetic pathway leading to the formation of the neurotoxin, β-L-oxalyl-2,3-diaminopropionic acid (β-L-ODAP). The final reaction of the pathway depends on an interaction between L. sativus acyl-activating enzyme 3 (LsAAE3) and a BAHD-acyltransferase (LsBOS) that form a metabolon activated by CoA to produce β-L-ODAP. This provides valuable insight into the best approaches for developing varieties which produce substantially less toxin.
AB - Grass pea (Lathyrus sativus L.) is a rich source of protein cultivated as an insurance crop in Ethiopia, Eritrea, India, Bangladesh, and Nepal. Its resilience to both drought and flooding makes it a promising crop for ensuring food security in a changing climate. The lack of genetic resources and the crop’s association with the disease neurolathyrism have limited the cultivation of grass pea. Here, we present an annotated, long read-based assembly of the 6.5 Gbp L. sativus genome. Using this genome sequence, we have elucidated the biosynthetic pathway leading to the formation of the neurotoxin, β-L-oxalyl-2,3-diaminopropionic acid (β-L-ODAP). The final reaction of the pathway depends on an interaction between L. sativus acyl-activating enzyme 3 (LsAAE3) and a BAHD-acyltransferase (LsBOS) that form a metabolon activated by CoA to produce β-L-ODAP. This provides valuable insight into the best approaches for developing varieties which produce substantially less toxin.
UR - http://www.scopus.com/inward/record.url?scp=85148254990&partnerID=8YFLogxK
U2 - 10.1038/s41467-023-36503-2
DO - 10.1038/s41467-023-36503-2
M3 - Article
SN - 2041-1723
VL - 14
JO - Nature Communications
JF - Nature Communications
M1 - 876
ER -