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Related Experiment Videos

Mn(II) binding by the anthracis repressor from Bacillus anthracis.

K Ilker Sen1, Andrzej Sienkiewicz, John F Love

  • 1Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.

Biochemistry
|March 29, 2006
PubMed
Summary
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The anthracis repressor (AntR), a manganese-activated regulator, binds two manganese ions with positive cooperativity. AntR forms a dimer, providing insights into DtxR protein family metal activation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The anthracis repressor (AntR) is a manganese-activated transcriptional regulator.
  • AntR belongs to the diphtheria toxin repressor (DtxR) protein family.

Purpose of the Study:

  • To characterize the manganese(II) (Mn(II)) binding properties of AntR.
  • To investigate the dimerization state of AntR in the presence and absence of Mn(II).

Main Methods:

  • Continuous wave (cw) and pulsed Electron Paramagnetic Resonance (EPR) spectroscopy.
  • Stopped-flow EPR for kinetic measurements.
  • Equilibrium metal binding experiments.
  • Size exclusion chromatography and double electron-electron resonance (DEER) EPR.

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Main Results:

  • AntR binds two Mn(II) ions with positive cooperativity and distinct dissociation constants (210 and 16.6 µM).
  • Mn(II) on-rates are sub-millisecond, and dissociation is biphasic (35.7 and 0.115 s⁻¹).
  • EPR data indicate the two Mn(II) ions do not form a binuclear cluster.
  • AntR exists as a dimer in the absence of Mn(II).

Conclusions:

  • These findings elucidate the metal activation mechanism of AntR.
  • The results facilitate comparisons with other DtxR family proteins.