Analysis of trehalose-6-phosphate synthase (TPS) gene family suggests the formation of TPS complexes in rice |
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Authors: | Baisheng Zang Haowen Li Wenjun Li Xing Wang Deng Xiping Wang |
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Institution: | (1) Peking-Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology, National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing, 100871, People’s Republic of China;(2) Beijing Key Laboratory of Gene Engineering Drug and Biotechnology, Key Laboratory of Cell Proliferation and Regulation Biology Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, 100875, People’s Republic of China;(3) State Key Laboratory of Genetic Engineering, Fudan University, Shanghai, 200433, People’s Republic of China;(4) Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520, USA;(5) National Center for Molecular Crop Design, Weiming Kaituo Agriculture Biotech Co., Ltd, Beijing, 100085, People’s Republic of China; |
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Abstract: | Trehalose-6-phosphate (T6P), an intermediate in the trehalose biosynthesis pathway, is emerging as an important regulator
of plant metabolism and development. T6P levels are potentially modulated by a group of trehalose-6-phosphate synthase (TPS)
and trehalose-6-phosphate phosphatase (TPP) homologues. In this study, we have isolated 11 TPS genes encoding proteins with both TPS and TPP domains, from rice. Functional complement assays performed in yeast tps1 and tps2 mutants, revealed that only OsTPS1 encodes an active TPS enzyme and no OsTPS protein possesses TPP activity. By using a yeast two-hybrid analysis, a complicated
interaction network occurred among OsTPS proteins, and the TPS domain might be essential for this interaction to occur. The
interaction between OsTPS1 and OsTPS8 in vivo was confirmed by bimolecular fluorescence complementation and coimmunoprecipitation
assays. Furthermore, our gel filtration assay showed that there may exist two forms of OsTPS1 (OsTPS1a and OsTPS1b) with different
elution profiles in rice. OsTPS1b was particularly cofractionated with OsTPS5 and OsTPS8 in the 360 kDa complex, while OsTPS1a
was predominantly incorporated into the complexes larger than 360 kDa. Collectively, these results suggest that OsTPS family members may form trehalose-6-phosphate synthase complexes and therefore potentially modify T6P levels to regulate
plant development. |
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