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

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.

SUBMITTER: Goldfless SJ

PROVIDER: S-EPMC3351163 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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

Goldfless Stephen J SJ Belmont Brian J BJ de Paz Alexandra M AM Liu Jessica F JF Niles Jacquin C JC

Nucleic acids research 20120124 9

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 e ...[more]

PMID: 22275521

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2019-06-14 | GSE131668 | GEO

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