An essential role of caffeoyl shikimate esterase in monolignol biosynthesis in Medicago truncatula

Summary Biochemical and genetic analyses have previously identified caffeoyl shikimate esterase (CSE) as an enzyme in the monolignol biosynthesis pathway in Arabidopsis thaliana, although the generality of this finding has been questioned. Here we show the presence of CSE genes and associated enzyme...

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Veröffentlicht in:The Plant journal : for cell and molecular biology 2016-06, Vol.86 (5), p.363-375
Hauptverfasser: Ha, Chan Man, Escamilla‐Trevino, Luis, Yarce, Juan Carlos Serrani, Kim, Hoon, Ralph, John, Chen, Fang, Dixon, Richard A.
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Sprache:eng
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Zusammenfassung:Summary Biochemical and genetic analyses have previously identified caffeoyl shikimate esterase (CSE) as an enzyme in the monolignol biosynthesis pathway in Arabidopsis thaliana, although the generality of this finding has been questioned. Here we show the presence of CSE genes and associated enzyme activity in barrel medic (Medicago truncatula, dicot, Leguminosae), poplar (Populus deltoides, dicot, Salicaceae), and switchgrass (Panicum virgatum, monocot, Poaceae). Loss of function of CSE in transposon insertion lines of M. truncatula results in severe dwarfing, altered development, reduction in lignin content, and preferential accumulation of hydroxyphenyl units in lignin, indicating that the CSE enzyme is critical for normal lignification in this species. However, the model grass Brachypodium distachyon and corn (Zea mays) do not possess orthologs of the currently characterized CSE genes, and crude protein extracts from stems of these species exhibit only a weak esterase activity with caffeoyl shikimate. Our results suggest that the reaction catalyzed by CSE may not be essential for lignification in all plant species. Significance Statement The role of caffeoyl shikimate esterase in lignin biosynthesis is controversial. Here we show that its role in lignification differs significantly among species; it is totally dispensable in Brachypodium, significantly involved in Arabidopsis and critically involved in Medicago.
ISSN:0960-7412
1365-313X
DOI:10.1111/tpj.13177