Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

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

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)5369-5372
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume24
Issue number23
DOIs
Publication statusPublished - Dec 1 2014

Fingerprint

Biosynthesis
Protein Biosynthesis
Transfer RNA
Codon
Proteins
Peptide Elongation Factor Tu
Anticodon
Protein Engineering
Light
Amino Acids
Messenger RNA

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Molecular Biology
  • Molecular Medicine
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science
  • Medicine(all)

Cite this

Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA. / Akahoshi, Akiya; Doi, Yoshio; Sisido, Masahiko; Watanabe, Kazunori; Ohtsuki, Takashi.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 24, No. 23, 01.12.2014, p. 5369-5372.

Research output: Contribution to journalArticle

Akahoshi, Akiya ; Doi, Yoshio ; Sisido, Masahiko ; Watanabe, Kazunori ; Ohtsuki, Takashi. / Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA. In: Bioorganic and Medicinal Chemistry Letters. 2014 ; Vol. 24, No. 23. pp. 5369-5372.
@article{a5f83cd0e1744dbd95841a369c45d86c,
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",
year = "2014",
month = "12",
day = "1",
doi = "10.1016/j.bmcl.2014.10.053",
language = "English",
volume = "24",
pages = "5369--5372",
journal = "Bioorganic and Medicinal Chemistry Letters",
issn = "0960-894X",
publisher = "Elsevier Limited",
number = "23",

}

TY - JOUR

T1 - Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

AU - Akahoshi, Akiya

AU - Doi, Yoshio

AU - Sisido, Masahiko

AU - Watanabe, Kazunori

AU - Ohtsuki, Takashi

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

UR - http://www.scopus.com/inward/record.url?scp=84910155916&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84910155916&partnerID=8YFLogxK

U2 - 10.1016/j.bmcl.2014.10.053

DO - 10.1016/j.bmcl.2014.10.053

M3 - Article

C2 - 25453789

AN - SCOPUS:84910155916

VL - 24

SP - 5369

EP - 5372

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

SN - 0960-894X

IS - 23

ER -