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- W4247451811 abstract "The ykkC family of bacterial riboswitches combines several widespread classes that have similar secondary structures and consensus motifs but control different genes in response to different cellular metabolites. Here we report the crystal structures of two distinct ykkC riboswitches specifically bound to their cognate ligand ppGpp, a second messenger involved in stress response, or PRPP, a precursor in purine biosynthesis. Both RNAs adopt similar structures and contain a conserved core previously observed in the guanidine-specific ykkC riboswitch. However, ppGpp and PRPP riboswitches uniquely employ an additional helical element that joins the ends of the ligand-sensing domains and creates a tunnel for direct and Mg2+-mediated binding of ligands. Mutational and footprinting experiments highlight the importance of conserved nucleotides forming the tunnel and long-distance contacts for ligand binding and genetic response. Our work provides new insights into the specificity of riboswitches and gives a unique opportunity for future studies of RNA evolution. Structural analysis of PRPP and ppGpp riboswitches reveals that they employ a helical element to create a tunnel for the ligand, whose specificity is determined by the conserved nucleotides forming the tunnel and long-distance contacts." @default.
- W4247451811 created "2022-05-12" @default.
- W4247451811 creator A5023189510 @default.
- W4247451811 creator A5089150516 @default.
- W4247451811 date "2018-08-17" @default.
- W4247451811 modified "2023-09-30" @default.
- W4247451811 title "ykkC riboswitches employ an add-on helix to adjust specificity for polyanionic ligands" @default.
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- W4247451811 doi "https://doi.org/10.1038/s41589-018-0114-4" @default.
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