Journal
NUCLEIC ACIDS RESEARCH
Volume 40, Issue 9, Pages -Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gks028
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Funding
- National Institutes of Health, NIH [1DP2OD007124]
- National Institute of Environmental Health Sciences [5-T32-ES007020]
- National Science Foundation, Research Experiences for Undergraduates [1005055]
- MIT
- Direct For Biological Sciences
- Div Of Biological Infrastructure [1005055] Funding Source: National Science Foundation
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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.
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