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

Abstract:

: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.

authors

Uhm H,Kang W,Ha KS,Kang C,Hohng S

doi

10.1073/pnas.1712983115

subject

Has Abstract

pub_date

2018-01-09 00:00:00

pages

331-336

issue

2

eissn

0027-8424

issn

1091-6490

pii

1712983115

journal_volume

115

pub_type

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