Roles of Mg2+ in TPP-dependent riboswitch

FEBS Lett. 2005 May 9;579(12):2583-8. doi: 10.1016/j.febslet.2005.03.074. Epub 2005 Apr 8.

Abstract

We quantified the effect of Mg(2+) on thiamine pyrophosphate (TPP) binding to TPP-dependent thiA riboswitch RNA. The association constant of TPP binding to the riboswitch at 20 degrees C increased from 1.2 x 10(6) to 50 x 10(6) M(-1) as the Mg(2+) concentration increased from 0 to 1 mM. Furthermore, circular dichroic spectra under various conditions showed that 1 mM Mg(2+) induced a local structural change of the riboswitch, which might be pivotal for TPP binding. These results indicate that a physiological concentration of Mg(2+) can regulate TPP binding to the thiA riboswitch.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5' Untranslated Regions
  • Adenosine / metabolism
  • Base Sequence
  • Binding Sites
  • Circular Dichroism
  • Conserved Sequence
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression Regulation
  • Kinetics
  • Magnesium / metabolism*
  • Magnesium / pharmacology
  • Magnesium / physiology
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • RNA / chemistry
  • RNA / classification
  • RNA / genetics
  • RNA / metabolism*
  • Sequence Analysis, RNA
  • Sequence Homology, Nucleic Acid
  • Temperature
  • Thiamine Pyrophosphate / metabolism*
  • Titrimetry
  • Transcription, Genetic

Substances

  • 5' Untranslated Regions
  • RNA
  • Magnesium
  • Adenosine
  • Thiamine Pyrophosphate