Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers.

Ítems similars

• Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.
  per: Schiering, N, et al.
  Publicat: (1995)
• Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence.
  per: Tao, X, et al.
  Publicat: (1992)
• Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection.
  per: Tao, X, et al.
  Publicat: (1994)
• Mechanism of metal ion activation of the diphtheria toxin repressor DtxR
  per: D'Aquino, J. Alejandro, et al.
  Publicat: (2005)
• Metal stoichiometry and functional studies of the diphtheria toxin repressor
  per: Spiering, Michelle M., et al.
  Publicat: (2003)