Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

Akiya Akahoshi; Yoshio Doi; Masahiko Sisido; Kazunori Watanabe; Takashi Ohtsuki

doi:10.1016/j.bmcl.2014.10.053

Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

Akiya Akahoshi, Yoshio Doi, Masahiko Sisido, Kazunori Watanabe, Takashi Ohtsuki

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Translation systems with four-base codons provide a powerful strategy for protein engineering and protein studies because they enable site-specific incorporation of non-natural amino acids into proteins. In this study, a caged aminoacyl-tRNA with a four-base anticodon was synthesized. The caged aminoacyl-tRNA contains a photocleavable nitroveratryloxycarbonyl (NVOC) group. This study showed that the caged aminoacyl-tRNA was not deacylated, did not bind to EF-Tu, and was activated by light. Photo-dependent translation of an mRNA containing the four-base codon was demonstrated using the caged aminoacyl-tRNA.

Original language	English
Pages (from-to)	5369-5372
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	24
Issue number	23
DOIs	https://doi.org/10.1016/j.bmcl.2014.10.053
Publication status	Published - Dec 1 2014

Keywords

Caged aminoacyl-tRNA
Non-natural amino acid
Photocleavable group
Site-specific incorporation
Translation

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2014.10.053

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title = "Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA",

abstract = "Translation systems with four-base codons provide a powerful strategy for protein engineering and protein studies because they enable site-specific incorporation of non-natural amino acids into proteins. In this study, a caged aminoacyl-tRNA with a four-base anticodon was synthesized. The caged aminoacyl-tRNA contains a photocleavable nitroveratryloxycarbonyl (NVOC) group. This study showed that the caged aminoacyl-tRNA was not deacylated, did not bind to EF-Tu, and was activated by light. Photo-dependent translation of an mRNA containing the four-base codon was demonstrated using the caged aminoacyl-tRNA.",

keywords = "Caged aminoacyl-tRNA, Non-natural amino acid, Photocleavable group, Site-specific incorporation, Translation",

author = "Akiya Akahoshi and Yoshio Doi and Masahiko Sisido and Kazunori Watanabe and Takashi Ohtsuki",

note = "Funding Information: This work was supported by a Grant-in-Aid for Scientific Research on Innovative Areas {\textquoteleft}Nanomedicine Molecular Science{\textquoteright} (Grant number 26107711 ) from MEXT , Japan. Publisher Copyright: {\textcopyright} 2014 Elsevier Ltd. All rights reserved. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",

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doi = "10.1016/j.bmcl.2014.10.053",

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AU - Akahoshi, Akiya

AU - Doi, Yoshio

AU - Sisido, Masahiko

AU - Watanabe, Kazunori

AU - Ohtsuki, Takashi

N1 - Funding Information: This work was supported by a Grant-in-Aid for Scientific Research on Innovative Areas ‘Nanomedicine Molecular Science’ (Grant number 26107711 ) from MEXT , Japan. Publisher Copyright: © 2014 Elsevier Ltd. All rights reserved. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.

PY - 2014/12/1

Y1 - 2014/12/1

N2 - Translation systems with four-base codons provide a powerful strategy for protein engineering and protein studies because they enable site-specific incorporation of non-natural amino acids into proteins. In this study, a caged aminoacyl-tRNA with a four-base anticodon was synthesized. The caged aminoacyl-tRNA contains a photocleavable nitroveratryloxycarbonyl (NVOC) group. This study showed that the caged aminoacyl-tRNA was not deacylated, did not bind to EF-Tu, and was activated by light. Photo-dependent translation of an mRNA containing the four-base codon was demonstrated using the caged aminoacyl-tRNA.

AB - Translation systems with four-base codons provide a powerful strategy for protein engineering and protein studies because they enable site-specific incorporation of non-natural amino acids into proteins. In this study, a caged aminoacyl-tRNA with a four-base anticodon was synthesized. The caged aminoacyl-tRNA contains a photocleavable nitroveratryloxycarbonyl (NVOC) group. This study showed that the caged aminoacyl-tRNA was not deacylated, did not bind to EF-Tu, and was activated by light. Photo-dependent translation of an mRNA containing the four-base codon was demonstrated using the caged aminoacyl-tRNA.

KW - Caged aminoacyl-tRNA

KW - Non-natural amino acid

KW - Photocleavable group

KW - Site-specific incorporation

KW - Translation

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JO - Bioorganic and Medicinal Chemistry Letters

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Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

Abstract

Keywords

ASJC Scopus subject areas

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