Journal
JOURNAL OF BIOCHEMISTRY
Volume 156, Issue 6, Pages 323-331Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvu048
Keywords
allosteric control; aptamer; cooperativity; genetic circuit; glycine riboswitch
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Funding
- University of Central Florida
- National Cancer Institute at the National Institutes of Health [R21CA175625]
- NATIONAL CANCER INSTITUTE [R21CA175625] Funding Source: NIH RePORTER
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Glycine riboswitches contain two aptamers and turn on the expression of downstream genes in bacteria. Although full-length glycine riboswitches were shown to exhibit no glycine-binding cooperativity, the truncated glycine riboswitches were confirmed to bind two glycine molecules cooperatively. Thorough understanding of the ligand-binding cooperativity may shed light on the molecular basis of the cooperativity and help design novel intricate biosensing genetic circuits for application in synthetic biology. A previously proposed sequential model does not readily provide explanation for published data showing a deleterious mutation in the first aptamer inhibiting the glycine binding of the second one. Using the glycine riboswitch from Vibrio cholerae as a model system, we have identified a region in the first aptamer that modulates the second aptamer function especially in the shortened glycine riboswitch. Importantly, this modulation can be rescued by the addition of a complementary oligodeoxynucleotide, demonstrating the feasibility of developing this system into novel genetic circuits that sense both glycine and a DNA signal.
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