An unnatural base pair for incorporating amino acid analogs into proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-02

AUTHORS

Ichiro Hirao, Takashi Ohtsuki, Tsuyoshi Fujiwara, Tsuneo Mitsui, Tomoko Yokogawa, Taeko Okuni, Hiroshi Nakayama, Koji Takio, Takashi Yabuki, Takanori Kigawa, Koichiro Kodama, Takashi Yokogawa, Kazuya Nishikawa, Shigeyuki Yokoyama

ABSTRACT

An unnatural base pair of 2-amino-6-(2-thienyl)purine (denoted by s) and pyridin-2-one (denoted by y) was developed to expand the genetic code. The ribonucleoside triphosphate of y was site-specifically incorporated into RNA, opposite s in a template, by T7 RNA polymerase. This transcription was coupled with translation in an Escherichia coli cell-free system. The yAG codon in the transcribed ras mRNA was recognized by the CUs anticodon of a yeast tyrosine transfer RNA (tRNA) variant, which had been enzymatically aminoacylated with an unnatural amino acid, 3-chlorotyrosine. Site-specific incorporation of 3-chlorotyrosine into the Ras protein was demonstrated by liquid chromatography-mass spectrometry (LC-MS) analysis of the products. This coupled transcription-translation system will permit the efficient synthesis of proteins with a tyrosine analog at the desired position. More... »

PAGES

177-182

Journal

TITLE

Nature Biotechnology

ISSUE

2

VOLUME

20

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt0202-177

    DOI

    http://dx.doi.org/10.1038/nbt0202-177

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1043282175

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11821864


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