The reconstruction and biochemical characterization of ancestral genes furnish insights into the evolution of terpene synthase function in the Poaceae

Plant Molecular Biology
Katrin LuckTobias G Köllner

Abstract

Distinct catalytic features of the Poaceae TPS-a subfamily arose early in grass evolution and the reactions catalyzed have become more complex with time. The structural diversity of terpenes found in nature is mainly determined by terpene synthases (TPS). TPS enzymes accept ubiquitous prenyl diphosphates as substrates and convert them into the various terpene skeletons by catalyzing a carbocation-driven reaction. Based on their sequence similarity, terpene synthases from land plants can be divided into different subfamilies, TPS-a to TPS-h. In this study, we aimed to understand the evolution and functional diversification of the TPS-a subfamily in the Poaceae (the grass family), a plant family that contains important crops such as maize, wheat, rice, and sorghum. Sequence comparisons showed that aside from one clade shared with other monocot plants, the Poaceae TPS-a subfamily consists of five well-defined clades I-V, the common ancestor of which probably originated very early in the evolution of the grasses. A survey of the TPS literature and the characterization of representative TPS enzymes from clades I-III revealed clade-specific substrate and product specificities. The enzymes in both clade I and II function as sesquiterp...Continue Reading

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Citations

Jul 3, 2021·International Journal of Molecular Sciences·Dongmei LiangJianjun Qiao

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Datasets Mentioned

BETA
MT294265
MT294266
MT294267
MT294268
MT294269
MT294270
MT294271
MT294272

Methods Mentioned

BETA
transgenic

Software Mentioned

BLASTP
Guidance
TBLASTN
MUSCLE
ExtAncSeqMEGA
MEGA6

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