ID | 54548 |
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Author |
Ohtsuki, Takashi
Department of Biomedical Engineering, Okayama University
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Kanzaki, Shigeto
Department of Biomedical Engineering, Okayama University
Nishimura, Sae
Department of Biomedical Engineering, Okayama University
Kunihiro, Yoshio
Department of Biomedical Engineering, Okayama University
Sisido, Masahiko
Department of Biomedical Engineering, Okayama University
Watanabe, Kazunori
Department of Biomedical Engineering, Okayama University
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Abstract | The possibility of spatiotemporally photocontrolling translation holds considerable promise for studies on the biological roles of local translation in cells and tissues. Here we report caged aminoacyl-tRNAs (aa-tRNAs) synthesized using a (7-diethylaminocoumarin-4-yl)methoxycarbonyl (DEACM)-cage compound. DEACM-caged aa-tRNA does not spontaneously deacylate for at least 4 h in neutral aqueous solution, and does not bind to the elongation factor Tu. On irradiation at ∼405 nm at 125 mW cm(-2), DEACM-aa-tRNA is converted into active aa-tRNA with a half-life of 19 s. Notably, this rapid uncaging induced by visible light does not impair the translation system. Translation is photoinduced when DEACM-aa-tRNA carrying a CCCG or a CUA anticodon is uncaged in the presence of mRNAs harbouring a CGGG four-base codon or a UAG amber codon, respectively. Protein synthesis is phototriggered in several model systems, including an in vitro translation system, an agarose gel, in liposomes and in mammalian cells.
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Note | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
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Published Date | 2016-08
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Publication Title |
Nature Communications
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Volume | volume7
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Publisher Alternative | Macmillan Publishers Limited, part of Springer Nature
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Start Page | 12501
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End Page | 12501
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ISSN | 2041-1723
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NCID | AA12645905
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Content Type |
Journal Article
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Official Url | http://www.nature.com/ncomms/
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language |
English
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Copyright Holders | © The Author(s) 2016
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File Version | publisher
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Refereed |
True
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