• Title/Summary/Keyword: Enhanced yellow fluorescent protein

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A novel technique for recombinant protein expression in duckweed (Spirodela polyrhiza) turions

  • Chanroj, Salil;Jaiprasert, Aornpilin;Issaro, Nipatha
    • Journal of Plant Biotechnology
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    • v.48 no.3
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    • pp.156-164
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    • 2021
  • Spirodela polyrhiza, from the Lemnaceae family, are small aquatic plants that offer an alternative plant-based system for the expression of recombinant proteins. However, no turion transformation protocol has been established in this species. In this study, we exploited a pB7YWG2 vector harboring the eYFP gene that encodes enhanced yellow fluorescent protein (eYFP), which has been extensively used as a reporter and marker to visualize recombinant protein localization in plants. We adopted Agrobacterium tumefaciens-mediated turion transformation via vacuum infiltration to deliver the eYFP gene to turions, special vegetative forms produced by duckweeds to endure harsh conditions. Transgenic turions regenerated several duckweed fronds that exhibited yellow fluorescent emissions under a fluorescence microscope. Western blotting verified the expression of the eYFP protein. To the best of our knowledge, this is the first report of an efficient protocol for generating transgenic S. polyrhiza expressing eYFP via Agrobacterium tumefaciens-mediated turion transformation. The ability of turions to withstand harsh conditions increases the portability and versatility of transgenic duckweeds, favoring their use in the further development of therapeutic compounds in plants.

Production of the yellow fluorescent silk using the fibroin heavy chain protein expression system in transgenic silkworm (피브로인 H-chain 재조합 단백질 발현시스템을 이용한 황색형광실크의 제작)

  • Kim, Seong Wan;Choi, Kwang-Ho;Kim, Seong Ryul;Yun, Eun Young;Park, Seung Won;Kang, Seok Woo;Goo, Tae Won
    • Journal of Sericultural and Entomological Science
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    • v.52 no.2
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    • pp.102-109
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    • 2014
  • We constructed the fibroin H-chain expression system to produce enhanced yellow fluorescent proteins (EYFP) in the silk of transgenic silkworm. Fluorescent silk could be made by fusing EYFP cDNA to the heavy chain gene and injecting it into a silkworm. The EYFP fusion protein, each with N- and C-terminal sequences of the fibroin H-chain, was designed to be secreted into the lumen of the posterior silk glands. The expression of the EYFP/H-chain fusion gene was regulated by the fibroin H-chain promoter. The yellow fluorescence proving that the fusion protein was present in the silk. Accordingly, we suggest that the EYFP fluorescence silk will enable the production of novel biomaterial based on the transgenic silk.