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Evolution of a Secondary Metabolic Pathway from Primary Metabolism: Shikimate and quinate biosynthesis in plants

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dc.contributor.author Carrington, Yuriko
dc.contributor.author Guo, Jia
dc.contributor.author Le, Cuong H.
dc.contributor.author Fillo, Alexander
dc.contributor.author Kwon, Junsu
dc.contributor.author Tran, Lan T.
dc.contributor.author Ehlting, Jurgen
dc.date.accessioned 2018-11-02T08:09:06Z
dc.date.copyright 2018 en_US
dc.date.issued 2018-06
dc.identifier.citation Carrington, Y., Guo, J., Le, C.H., Fillo, A., Kwon, J., Tran, L.T. & Ehlting, J. (2018). Evolution of a secondary metabolic pathway from primary metabolism: shikimate and quinate biosynthesis in plants. The Plant Journal, 95(5), 823-833. https://doi.org/10.1111/tpj.13990 en_US
dc.identifier.uri https://doi.org/10.1111/tpj.13990
dc.identifier.uri https://dspace.library.uvic.ca//handle/1828/10229
dc.description.abstract The shikimate pathway synthesizes aromatic amino acids essential for protein biosynthesis. Shikimate dehydrogenase (SDH) is a central enzyme of this primary metabolic pathway, producing shikimate. The structurally similar quinate is a secondary metabolite synthesized by quinate dehydrogenase (QDH). SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, represented here by Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in P. taeda maintained specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displayed a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH was sufficient to gain some QDH function. Thus, very few mutations were necessary to facilitate the evolution of QDH genes. en_US
dc.description.sponsorship This work has been supported by a Discovery Grant (to JE) from the Natural Sciences and Engineering Research Council of Canada (NSERC). YC was supported by a stipend from the NSERC Collaborative Research and Training Experience (CREATE) Program in Forests and Climate Change. AF and JK received undergraduate research project awards from the Centre for Forest Biology at the University of Victoria. We appreciate early access to the 1KP transcriptome database. en_US
dc.language.iso en en_US
dc.publisher the Plant Journal en_US
dc.subject molecular evolution en_US
dc.subject secondary metabolism en_US
dc.subject shikimate/quinate dehydrogenase en_US
dc.subject Rhodopirellula baltica en_US
dc.subject Chlamydomonas reinhardtii en_US
dc.subject Physcomitrella patens en_US
dc.subject Selaginella moellendorfii en_US
dc.subject Pinus taeda en_US
dc.subject Populus trichocarpa en_US
dc.title Evolution of a Secondary Metabolic Pathway from Primary Metabolism: Shikimate and quinate biosynthesis in plants en_US
dc.type Postprint en_US
dc.description.scholarlevel Faculty en_US
dc.description.reviewstatus Reviewed en_US
dc.description.embargo 2019-07-01


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