期刊
COMMUNICATIONS BIOLOGY
卷 4, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s42003-021-01739-5
关键词
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资金
- Japan Society for the Promotion of Science (JSPS) [16H00783, 17H05732, 18K06094, 19H04735, 19K07582]
- Yamada Science Foundation
- Eno Science Foundation
- New Energy and Industrial Technology Development Organization (NEDO) Japan
- Photon Factory and SPring-8 Program Advisory Committee [2017A6748, 2017A2570, 2017B6748, 2018A2719, 2018A6859, 2017G702]
- Grants-in-Aid for Scientific Research [17H05732, 18K06094, 16H00783, 19K07582, 19H04735] Funding Source: KAKEN
The study identified three novel Eucommia ulmoides TPT isoforms that synthesized TPI in vitro, with one of them showing a dimeric structure. Mutation analysis revealed the essential role of two amino acids in TPI biosynthesis, and spatiotemporal analysis indicated the involvement of TPI in seed development and maturation in Eucommia ulmoides.
Some plant trans-1,4-prenyltransferases (TPTs) produce ultrahigh molecular weight trans-1,4-polyisoprene (TPI) with a molecular weight of over 1.0 million. Although plant-derived TPI has been utilized in various industries, its biosynthesis and physiological function(s) are unclear. Here, we identified three novel Eucommia ulmoides TPT isoforms-EuTPT1, 3, and 5, which synthesized TPI in vitro without other components. Crystal structure analysis of EuTPT3 revealed a dimeric architecture with a central hydrophobic tunnel. Mutation of Cys94 and Ala95 on the central hydrophobic tunnel no longer synthesizd TPI, indicating that Cys94 and Ala95 were essential for forming the dimeric architecture of ultralong-chain TPTs and TPI biosynthesis. A spatiotemporal analysis of the physiological function of TPI in E. ulmoides suggested that it is involved in seed development and maturation. Thus, our analysis provides functional and mechanistic insights into TPI biosynthesis and uncovers biological roles of TPI in plants.
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