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Proc. Natl. Acad. Sci. USA, Published online before print December 26, 2017 | doi: 10.1073/pnas.1712983115 Single-molecule FRET studies on the cotranscriptional folding of a thiamine pyrophosphate riboswitch

Heesoo Uhm^a,b,c, Wooyoung Kang^a,b,c, Kook Sun Ha^d, Changwon Kang^e, and Sungchul Hohng^a,b,c,1^aDepartment of Physics and Astronomy, Seoul National University, Seoul 08826, Republic of Korea;

^bInstitute of Applied Physics, Seoul National University, Seoul 08826, Republic of Korea;

^cNational Center of Creative Research Initiatives, Seoul National University, Seoul 08826, Republic of Korea;

^dDepartment of Life Science, The University of Suwon, Gyeonggi-do 18323, Republic of Korea;

^eDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea
¹To whom correspondence should be addressed.

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.

thiamine pyrophosphate riboswitch, single-molecule FRET, cotranscriptional folding

논문정보

형식Research article
게재일2017년 12월 (BRIC 등록일 2018-01-03)
연구진국내 연구진
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