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Roles of Mg 2+ in TPP‐dependent riboswitch
Author(s) -
Yamauchi Takahiro,
Miyoshi Daisuke,
Kubodera Takafumi,
Nishimura Akira,
Nakai Susumu,
Sugimoto Naoki
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.074
Subject(s) - riboswitch , chemistry , binding site , stereochemistry , rna , thiamine pyrophosphate , biophysics , biochemistry , biology , cofactor , enzyme , non coding rna , gene
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 °C increased from 1.2 × 10 6 to 50 × 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.
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