Structural highlights
Publication Abstract from PubMed
Gene regulation in cis by riboswitches is prevalent in bacteria. The yybP-ykoY riboswitch family is quite widespread, yet its ligand and function remained unknown. Here, we characterize the Lactococcus lactis yybP-ykoY orphan riboswitch as a Mn(2+)-dependent transcription-ON riboswitch, with a approximately 30-40 muM affinity for Mn(2+). We further determined its crystal structure at 2.7 A to elucidate the metal sensing mechanism. The riboswitch resembles a hairpin, with two coaxially stacked helices tethered by a four-way junction and a tertiary docking interface. The Mn(2+)-sensing region, strategically located at the highly conserved docking interface, has two metal binding sites. Whereas one site tolerates the binding of either Mg(2+) or Mn(2+), the other site strongly prefers Mn(2+) due to a direct contact from the N7 of an invariable adenosine. Mutagenesis and a Mn(2+)-free E. coli yybP-ykoY structure further reveal that Mn(2+) binding is coupled with stabilization of the Mn(2+)-sensing region and the aptamer domain.
Mn(2+)-Sensing Mechanisms of yybP-ykoY Orphan Riboswitches.,Price IR, Gaballa A, Ding F, Helmann JD, Ke A Mol Cell. 2015 Mar 19;57(6):1110-23. doi: 10.1016/j.molcel.2015.02.016. PMID:25794619[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Price IR, Gaballa A, Ding F, Helmann JD, Ke A. Mn(2+)-Sensing Mechanisms of yybP-ykoY Orphan Riboswitches. Mol Cell. 2015 Mar 19;57(6):1110-23. doi: 10.1016/j.molcel.2015.02.016. PMID:25794619 doi:http://dx.doi.org/10.1016/j.molcel.2015.02.016
