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

Saki Inuzuka, Hitoshi Kakizawa, Kei Ichiro Nishimura, Takuto Naito, Katsushi Miyazaki, Hiroyuki Furuta, Shigeyoshi Matsumura, Yoshiya Ikawa

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)435-447
    Number of pages13
    JournalGenes to Cells
    Volume23
    Issue number6
    DOIs
    Publication statusPublished - Jun 2018

    All Science Journal Classification (ASJC) codes

    • Genetics
    • Cell Biology

    Fingerprint

    Dive into the research topics of 'Recognition of cyclic-di-GMP by a riboswitch conducts translational repression through masking the ribosome-binding site distant from the aptamer domain'. Together they form a unique fingerprint.

    Cite this