Journal
CHEMISTRY & BIOLOGY
Volume 21, Issue 2, Pages 205-216Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2013.11.012
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Funding
- National Institutes of Health [R01 GM073850]
- predoctoral Creative Training in Molecular Biology Grant [NIH 5-T32-GM07135]
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The tetrahydrofolate (THF) riboswitch regulates folate transport and metabolism in a number of Firmicutes by cooperatively binding two molecules of THF. To further understand this riboswitch's specificity for THF, binding and regulatory activity of a series of THF analogs and antifolates were examined. Our data reveal that although binding is dominated by the RNA's interactions with the pterin moiety, the para-aminobenzoic acid (pABA) moiety plays a significant role in transcriptional regulation. Further, we find that adenine and several other analogs bind with high affinity by an alternative binding mechanism. Despite a similar affinity to THF, adenine is a poor regulator of transcriptional attenuation. These results demonstrate that binding alone does not determine a compound's effectiveness in regulating the activity of the riboswitch-a complication in current efforts to develop antimicrobials that target these RNAs.
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