Synthesis of Short-chain-length/Medium-chain-length Polyhydroxyalkanoate (PHA) Copolymers in Peroxisome of the Transgenic Arabidopsis Thaliana Harboring the PHA Synthase Gene from Pseudomonas sp. 61-3 |
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Authors: | Ken’ichiro Matsumoto Yuko Arai Rina Nagao Takaaki Murata Kazuma Takase Hideo Nakashita Seiichi Taguchi Hiroaki Shimada Yoshiharu Doi |
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Institution: | (1) Department of Biological Science and Technology, Tokyo University of Science, Yamazaki 2641, Noda, Chiba 278-8510, Japan;(2) Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan;(3) National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki 444-8585, Japan;(4) Division of Molecular Chemistry, Graduate School of Engineering, Hokkaido University, Sapporo 060-8628, Japan;(5) Division of Plant Biotechnology, Tissue Engineering Research Center, Tokyo University of Science, Tokyo, Japan |
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Abstract: | In this paper, the photosynthetic production of short-chain-length/medium-chain-length polyhydroxyalkanoate (PHA) copolymers is reported. The wild-type and highly active doubly mutated PHA synthase 1 (S325T/Q481K, abbreviated ST/QK) genes from Pseudomonas sp. 61-3 were introduced into Arabidopsis thaliana. Peroxisome targeting signal 1 (PTS1) was used to target PHA synthases into the peroxisome to synthesize PHA from the intermediates of the β-oxidation pathway. The transgenic Arabidopsis produced PHA copolymers consisting of 40–57 mol% 3-hydroxybutyrate, 21–49 mol% 3-hydroxyvalerate, 8–18 mol% 3-hydroxyhexanoate, and 2–8 mol% 3-hydroxyoctanoate. The maximum PHA contents were 220μ g/g cell dry weight (cdw) in leaves, and 36μ g/g cdw in stems, respectively. The expression of the ST/QK mutated PHA synthase in leaves gene did not lead to significant difference in PHA content and monomer composition of PHAs, compared to the wild-type PHA synthase gene, suggesting that the supply of monomers may be a rate-determining step of PHA biosynthesis in the peroxisome. However, in stems, there were significant differences dependent on whether the wild-type or ST/QK mutated PHA synthase was expressed. These results suggest that tissue-specific monomer availability is important in determining the final mol% composition of PHA copolymers produced by the peroxisome in plants. |
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Keywords: | Polyhydroxyalkanoate Arabidopsis thaliana Peroxisome Pseudomonas sp 61-3 3-hydroxyvalerate |
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