Mengfei Lin1,2,3,4, Ruihu Jia1,2,3,4, Juncheng Li1,2,3,4, Mengjie Zhang1,2,3,4, Hanbin Chen1,2,3,4, Deng Zhang1,2,3,4, Junjie Zhang1,2,3,4, Xiaoyang Chen5,6,7,8. 1. State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, South China Agricultural University, Guangzhou, China. 2. Guangdong Key Laboratory for Innovative Development and Utilization of Forest Plant Germplasm, Guangzhou, China. 3. Guangdong Province Research Center of Woody Forage Engineering Technology, Guangzhou, China. 4. College of Forestry and Landscape Architecture, South China Agricultural University, Guangzhou, China. 5. State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, South China Agricultural University, Guangzhou, China. xychen@scau.edu.cn. 6. Guangdong Key Laboratory for Innovative Development and Utilization of Forest Plant Germplasm, Guangzhou, China. xychen@scau.edu.cn. 7. Guangdong Province Research Center of Woody Forage Engineering Technology, Guangzhou, China. xychen@scau.edu.cn. 8. College of Forestry and Landscape Architecture, South China Agricultural University, Guangzhou, China. xychen@scau.edu.cn.
Abstract
MAIN CONCLUSION: Moringa oleifera TPSs were genome-wide identified for the first time, and a phylogenetic analysis was performed to investigate evolutionary divergence. The qRT-PCR data show that MoTPS genes response to different stress treatments. The trehalose-6-phosphate synthase (TPS) family is involved in a wide range of stress-resistance processes in plants. Its direct product, trehalose-6-phosphate, acts as a specific signal of sucrose status and a regulator to modulate carbon metabolism within the plant. In this study, eight TPS genes were identified and cloned based on the M. oleifera genome; only MoTPS1 exhibited TPS activity among Group I proteins. The characteristics of the MoTPS gene family were determined by analyzing phylogenetic relationships, gene structures, conserved motifs, selective forces, and expression patterns. The Group II MoTPS genes were under relaxed purifying selection or positive selection. The glycosyltransferase family 20 domains generally had lower Ka/Ks ratios and nonsynonymous (Ka) changes compared with those of trehalose-phosphatase domains, which is consistent with stronger purifying selection due to functional constraints in performing TPS enzyme activity. Phylogenetic analyses of TPS proteins from M. oleifera and 17 other plant species indicated that TPS were present before the monocot-dicot split, whereas Group II TPSs were duplicated after the separation of dicots and monocots. Quantitative real-time PCR analysis showed that the expression patterns of TPSs displayed group specificities in M. oleifera. Particularly, Group I MoTPS genes closely relate to reproductive development and Group II MoTPS genes closely relate to high temperature resistance in leaves, stem, stem tip and roots. This work provides a scientific classification of plant TPSs, dissects the internal relationships between their evolution and expressions, and promotes functional researches.
MAIN CONCLUSION: Moringa oleifera TPSs were genome-wide identified for the first time, and a phylogenetic analysis was performed to investigate evolutionary divergence. The qRT-PCR data show that MoTPS genes response to different stress treatments. The trehalose-6-phosphate synthase (TPS) family is involved in a wide range of stress-resistance processes in plants. Its direct product, trehalose-6-phosphate, acts as a specific signal of sucrose status and a regulator to modulate carbon metabolism within the plant. In this study, eight TPS genes were identified and cloned based on the M. oleifera genome; only MoTPS1 exhibited TPS activity among Group I proteins. The characteristics of the MoTPS gene family were determined by analyzing phylogenetic relationships, gene structures, conserved motifs, selective forces, and expression patterns. The Group II MoTPS genes were under relaxed purifying selection or positive selection. The glycosyltransferase family 20 domains generally had lower Ka/Ks ratios and nonsynonymous (Ka) changes compared with those of trehalose-phosphatase domains, which is consistent with stronger purifying selection due to functional constraints in performing TPS enzyme activity. Phylogenetic analyses of TPS proteins from M. oleifera and 17 other plant species indicated that TPS were present before the monocot-dicot split, whereas Group II TPSs were duplicated after the separation of dicots and monocots. Quantitative real-time PCR analysis showed that the expression patterns of TPSs displayed group specificities in M. oleifera. Particularly, Group I MoTPS genes closely relate to reproductive development and Group II MoTPS genes closely relate to high temperature resistance in leaves, stem, stem tip and roots. This work provides a scientific classification of plant TPSs, dissects the internal relationships between their evolution and expressions, and promotes functional researches.
Authors: Ekaterina Kuznetsova; Michael Proudfoot; Claudio F Gonzalez; Greg Brown; Marina V Omelchenko; Ivan Borozan; Liran Carmel; Yuri I Wolf; Hirotada Mori; Alexei V Savchenko; Cheryl H Arrowsmith; Eugene V Koonin; Aled M Edwards; Alexander F Yakunin Journal: J Biol Chem Date: 2006-09-21 Impact factor: 5.157
Authors: Jean E Harthill; Sarah E M Meek; Nick Morrice; Mark W Peggie; Jonas Borch; Barry H C Wong; Carol Mackintosh Journal: Plant J Date: 2006-06-08 Impact factor: 6.417
Authors: Umesh Prasad Yadav; Alexander Ivakov; Regina Feil; Guang You Duan; Dirk Walther; Patrick Giavalisco; Maria Piques; Petronia Carillo; Hans-Michael Hubberten; Mark Stitt; John Edward Lunn Journal: J Exp Bot Date: 2014-01-13 Impact factor: 6.992