Conformational capture of the SAM-II riboswitch. Academic Article uri icon

Overview

MeSH

  • Base Pairing
  • Fluorescence Resonance Energy Transfer
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Microscopy, Fluorescence
  • Nucleic Acid Conformation
  • Spectrometry, Fluorescence

MeSH Major

  • RNA, Bacterial
  • Riboswitch
  • S-Adenosylmethionine

abstract

  • Riboswitches are gene regulation elements in mRNA that function by specifically responding to metabolites. Although the metabolite-bound states of riboswitches have proven amenable to structure determination efforts, knowledge of the structural features of riboswitches in their ligand-free forms and their ligand-response mechanisms giving rise to regulatory control is lacking. Here we explore the ligand-induced folding process of the S-adenosylmethionine type II (SAM-II) riboswitch using chemical and biophysical methods, including NMR and fluorescence spectroscopy, and single-molecule fluorescence imaging. The data reveal that the unliganded SAM-II riboswitch is dynamic in nature, in that its stem-loop element becomes engaged in a pseudoknot fold through base-pairing with nucleosides in the 3' overhang containing the Shine-Dalgarno sequence. Although the pseudoknot structure is highly transient in the absence of its ligand, S-adenosylmethionine (SAM), it becomes conformationally restrained upon ligand recognition, through a conformational capture mechanism. These insights provide a molecular understanding of riboswitch dynamics that shed new light on the mechanism of riboswitch-mediated translational regulation.

publication date

  • June 2011

has subject area

  • Base Pairing
  • Fluorescence Resonance Energy Transfer
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Microscopy, Fluorescence
  • Nucleic Acid Conformation
  • RNA, Bacterial
  • Riboswitch
  • S-Adenosylmethionine
  • Spectrometry, Fluorescence

Research

keywords

  • Journal Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1038/nchembio.562

PubMed ID

  • 21532598

Additional Document Info

start page

  • 393

end page

  • 400

volume

  • 7

number

  • 6