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Nucleic Acids Research, Vol 27, Issue 16 3283-3290, Copyright © 1999 by Oxford University Press

ARTICLES

Facile characterization of translation initiation via nonsense codon suppression

AV Karginov, M Lodder and SM Hecht
Department of Chemistry and Department of Biology, University of Virginia, Charlottesville, VA 22901, USA.

A new strategy for studying the mechanism of translation initiation in eukaryotes has been developed. The strategy involves the use of an in vitro translation system to incorporate a non-natural fluorescent amino acid into a protein from a suppressor tRNAPheCUA misacylated with that amino acid. It is thereby possible to monitor translation initiation efficiency at an AUG codon in different contexts; this is illustrated for three constructs encoding Escherichia coli dihydrofolate reductase mRNA with different translation initiation regions. Fluorescence measurements after in vitro translation of the mRNAs in rabbit reticulocyte lysate reflected differences in the position and efficiency of translation initiation and, therefore, can be used for characterization of the translation initiation process.
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T. Hohsaka, Y. Ashizuka, H. Murakami, and M. Sisido
Five-base codons for incorporation of nonnatural amino acids into proteins
Nucleic Acids Res., September 1, 2001; 29(17): 3646 - 3651.
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