Journal
PLANT PHYSIOLOGY
Volume 170, Issue 4, Pages 1935-1944Publisher
OXFORD UNIV PRESS INC
DOI: 10.1104/pp.15.01813
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Funding
- Natural Sciences and Engineering Research Council of Canada Discovery Grant
- Canada Research Chairs
- Genome Canada
- Genome Alberta
- Genome Prairie
- Genome British Columbia
- Canada Foundation for Innovation
- Ontario Ministry of Research and Innovation
- National Research Council of Canada
- Consejo Nacional de Ciencia y Technologia, Mexico
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Members of the Apocynaceae plant family produce a large number of monoterpenoid indole alkaloids (MIAs) with different substitution patterns that are responsible for their various biological activities. A novel N-methyltransferase involved in the vindoline pathway in Catharanthus roseus showing distinct similarity to gamma-tocopherol C-methyltransferases was used in a bioinformatic screen of transcriptomes from Vinca minor, Rauvolfia serpentina, and C. roseus to identify 10 gamma-tocopherol-like N-methyltransferases from a large annotated transcriptome database of different MIA-producing plant species (www.phytometasyn.ca). The biochemical function of two members of this group cloned from V. minor (VmPiNMT) and R. serpentina (RsPiNMT) have been characterized by screening their biochemical activities against potential MIA substrates harvested from the leaf surfaces of MIA-accumulating plants. The approach was validated by identifying the MIA picrinine from leaf surfaces of Amsonia hubrichtii as a substrate of VmPiNMT and RsPiNMT. Recombinant proteins were shown to have high substrate specificity and affinity for picrinine, converting it to N-methylpicrinine (ervincine). Developmental studies with V. minor and R. serpentina showed that RsPiNMT and VmPiNMT gene expression and biochemical activities were highest in younger leaf tissues. The assembly of at least 150 known N-methylated MIAs within members of the Apocynaceae family may have occurred as a result of the evolution of the gamma-tocopherol-like N-methyltransferase family from gamma-tocopherol methyltransferases.
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