Gene regulation by a glycine riboswitch singlet uses a finely tuned energetic landscape for helical switching.

ABSTRACT: Riboswitches contain structured aptamer domains that, upon ligand binding, facilitate helical switching in their downstream expression platforms to alter gene expression. To fully dissect how riboswitches function requires a better understanding of the energetic landscape for helical switching. Here, we report a sequencing-based high-throughput assay for monitoring in vitro transcription termination and use it to simultaneously characterize the functional effects of all 522 single point mutants of a glycine riboswitch type-1 singlet. Mutations throughout the riboswitch cause ligand-dependent defects, but only mutations within the terminator hairpin alter readthrough efficiencies in the absence of ligand. A comprehensive analysis of the expression platform reveals that ligand binding stabil

SUBMITTER: Torgerson CD 

PROVIDER: S-EPMC6239177 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature