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Genes Cells. 2018 Jun;23(6):435-447. doi: 10.1111/gtc.12586. Epub 2018 Apr 25.

Recognition of cyclic-di-GMP by a riboswitch conducts translational repression through masking the ribosome-binding site distant from the aptamer domain.

Author information

1
Department of Chemistry, Graduate School of Science and Engineering, University of Toyama, Toyama, Japan.
2
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka, Japan.

Abstract

The riboswitch is a class of RNA-based gene regulatory machinery that is dependent on recognition of its target ligand by RNA tertiary structures. Ligand recognition is achieved by the aptamer domain, and ligand-dependent structural changes of the expression platform then usually mediate termination of transcription or translational initiation. Ligand-dependent structural changes of the aptamer domain and expression platform have been reported for several riboswitches with short (<40 nucleotides) expression platforms. In this study, we characterized structural changes of the Vc2 c-di-GMP riboswitch that represses translation of downstream open reading frames in a ligand-dependent manner. The Vc2 riboswitch has a long (97 nucleotides) expression platform, but its structure and function are largely unknown. Through mutational analysis and chemical probing, we identified its secondary structures that are possibly responsible for switch-OFF and switch-ON states of translational initiation.

KEYWORDS:

RNA ; aptamer; c-di-GMP; riboswitch; translational repression

PMID:
29693296
DOI:
10.1111/gtc.12586
[Indexed for MEDLINE]

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