Single-molecule FRET studies on the cotranscriptional folding of a thiamine pyrophosphate riboswitch

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Because RNAs fold as they are being synthesized, their transcription rate can affect their folding. Here, we report the results of single-molecule fluorescence studies that characterize the ligand-dependent cotranscriptional folding of the Escherichia coli thiM riboswitch that regulates translation. We found that the riboswitch aptamer folds into the "off" conformation independent of its ligand, but switches to the "on" conformation during transcriptional pausing near the translational start codon. Ligand binding maintains the riboswitch in the off conformation during transcriptional pauses. We expect our assay will permit the controlled study of the two main physical mechanisms that regulate cotranscriptional folding: transcriptional pausing and transcriptional speed.
Publisher
NATL ACAD SCIENCES
Issue Date
2018-01
Language
English
Article Type
Article
Keywords

THI-BOX RIBOSWITCH; ESCHERICHIA-COLI; TPP RIBOSWITCH; RNA-POLYMERASE; LIGAND RECOGNITION; ENERGY LANDSCAPE; GENE-EXPRESSION; TRANSCRIPTION; APTAMER; REVEAL

Citation

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.115, no.2, pp.331 - 336

ISSN
0027-8424
DOI
10.1073/pnas.1712983115
URI
http://hdl.handle.net/10203/240104
Appears in Collection
BS-Journal Papers(저널논문)
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