Metalloregulatory proteins: Metal selectivity and allosteric switching

Hermes Reyes-Caballero, Gregory C. Campanello, David P. Giedroc

Research output: Contribution to journalReview article

Abstract

Prokaryotic organisms have evolved the capacity to quickly adapt to a changing and challenging microenvironment in which the availability of both biologically required and non-essential transition metal ions can vary dramatically. In all bacteria, a panel of metalloregulatory proteins controls the expression of genes encoding membrane transporters and metal trafficking proteins that collectively manage metal homeostasis and resistance. These "metal sensors" are specialized allosteric proteins, in which the direct binding of a specific or small number of "cognate" metal ion(s) drives a conformational change in the regulator that allosterically activates or inhibits operator DNA binding, or alternatively, distorts the promoter structure thereby converting a poor promoter to a strong one. In this review, we discuss our current understanding of the features that control metal specificity of the allosteric response in these systems, and the role that structure, thermodynamics and conformational dynamics play in mediating allosteric activation or inhibition of DNA binding.

Original languageEnglish (US)
Pages (from-to)103-114
Number of pages12
JournalBiophysical Chemistry
Volume156
Issue number2-3
DOIs
StatePublished - Jul 1 2011

Keywords

  • Allostery
  • Energetics
  • Metal homeostasis
  • Protein-DNA interactions
  • Repressor
  • Transition metals

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry

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