Mutational analysis of structural elements in a class-I cyclic di-GMP riboswitch to elucidate its regulatory mechanism

Saki Inuzuka, Kei Ichiro Nishimura, Hitoshi Kakizawa, Yuki Fujita, Hiroyuki Furuta, Shigeyoshi Matsumura, Yoshiya Ikawa

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

The Vc2 riboswitch possesses an aptamer domain belonging to the class-I c-di-GMP riboswitch family. This domain has been analysed and the molecular mechanism by which it recognizes the c-di-GMP ligand has been elucidated. On the other hand, the regulatory mechanism of the full-length Vc2 riboswitch to control its downstream open reading frame (ORF) remains largely unknown. In this study, we performed in vivo reporter assays and in vitro biochemical analyses of the full-length riboswitch and its aptamer domain. We evaluated the results of in vivo and in vitro analyses to elucidate the regulatory mechanism of the Vc2 riboswitch. The present results suggest that recognition of c-di-GMP ligand by the Vc2 riboswitch aptamer domain downregulates expression of its downstream ORF primarily at the translational level.

Original languageEnglish
Pages (from-to)153-162
Number of pages10
JournalJournal of biochemistry
Volume160
Issue number3
DOIs
Publication statusPublished - Sep 1 2016

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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