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Nucleic Acids Res. 2012 May;40(9):e64. doi: 10.1093/nar/gks028. Epub 2012 Jan 24.

Direct and specific chemical control of eukaryotic translation with a synthetic RNA-protein interaction.

Author information

1
Department of Biological Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.

Abstract

Sequence-specific RNA-protein interactions, though commonly used in biological systems to regulate translation, are challenging to selectively modulate. Here, we demonstrate the use of a chemically-inducible RNA-protein interaction to regulate eukaryotic translation. By genetically encoding Tet Repressor protein (TetR)-binding RNA elements into the 5'-untranslated region (5'-UTR) of an mRNA, translation of a downstream coding sequence is directly controlled by TetR and tetracycline analogs. In endogenous and synthetic 5'-UTR contexts, this system efficiently regulates the expression of multiple target genes, and is sufficiently stringent to distinguish functional from non-functional RNA-TetR interactions. Using a reverse TetR variant, we illustrate the potential for expanding the regulatory properties of the system through protein engineering strategies.

PMID:
22275521
PMCID:
PMC3351163
DOI:
10.1093/nar/gks028
[Indexed for MEDLINE]
Free PMC Article

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