Communications Biology · 2019 · 52 citations · 54 references
The intracellular K<sup>+</sup> level in bacteria is strictly controlled by K<sup>+</sup> uptake and efflux systems. Among these, KdpFABC is a high-affinity K<sup>+</sup> transporter system that is generally activated by the KdpDE two-component system in response to K<sup>+</sup> limitation stress. However, the regulatory mechanism remains obscure in bacteria lacking the <i>kdpDE</i> genes. Here we report that the transcription of a <i>kdpFABC</i> operon is distinctively regulated by a cyclic diadenylate monophosphate (c-di-AMP) riboswitch located at the 5'-untranslated region of <i>kdp</i> transcript, and binding of c-di-AMP to the riboswitch promotes its intrinsic termination that blocks the <i>kdpFABC</i> transcription. Further, the intracellular c-di-AMP concentration was found to decrease under the K<sup>+</sup> limitation stress, leading to transcriptional read-through over the terminator to allow <i>kdpFABC</i> expression. This regulatory element is found predominantly in the <i>Bacillus cereus</i> group and correlate well with the K<sup>+</sup> and c-di-AMP homeostasis that affects a variety of crucial cellular functions.
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