Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-06

AUTHORS

Takatsugu Kobayashi, Osamu Nureki, Ryuichiro Ishitani, Anna Yaremchuk, Michael Tukalo, Stephen Cusack, Kensaku Sakamoto, Shigeyuki Yokoyama

ABSTRACT

The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do not cross-react with their bacterial counterparts. This 'orthogonal' condition is essential for using the archaeal pair to expand the bacterial genetic code. In this study, the structure of the Methanococcus jannaschii TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner using different residues. These diverse tRNA recognition modes form the basis for the orthogonality. The common tRNA(Tyr) identity determinants (the discriminator, A73 and the anticodon residues) are also recognized in manners different from those of the bacterial TyrRS. Based on this finding, we created a mutant TyrRS that aminoacylates the amber suppressor tRNA with C34 65 times more efficiently than does the wild-type enzyme. More... »

PAGES

425-432

Journal

TITLE

Nature Structural & Molecular Biology

ISSUE

6

VOLUME

10

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsb934

    DOI

    http://dx.doi.org/10.1038/nsb934

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1029733276

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12754495


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