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 language | English (US) |
|---|---|
| Pages (from-to) | 103-114 |
| Number of pages | 12 |
| Journal | Biophysical Chemistry |
| Volume | 156 |
| Issue number | 2-3 |
| DOIs | |
| State | Published - Jul 2011 |
| Externally published | Yes |
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Keywords
- Allostery
- Energetics
- Metal homeostasis
- Protein-DNA interactions
- Repressor
- Transition metals
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Organic Chemistry
Cite this
Metalloregulatory proteins : Metal selectivity and allosteric switching. / Reyes-Caballero, Hermes; Campanello, Gregory C.; Giedroc, David P.
In: Biophysical Chemistry, Vol. 156, No. 2-3, 07.2011, p. 103-114.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Metalloregulatory proteins
T2 - Metal selectivity and allosteric switching
AU - Reyes-Caballero, Hermes
AU - Campanello, Gregory C.
AU - Giedroc, David P.
PY - 2011/7
Y1 - 2011/7
N2 - 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.
AB - 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.
KW - Allostery
KW - Energetics
KW - Metal homeostasis
KW - Protein-DNA interactions
KW - Repressor
KW - Transition metals
UR - http://www.scopus.com/inward/record.url?scp=79956065205&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79956065205&partnerID=8YFLogxK
U2 - 10.1016/j.bpc.2011.03.010
DO - 10.1016/j.bpc.2011.03.010
M3 - Review article
C2 - 21511390
AN - SCOPUS:79956065205
VL - 156
SP - 103
EP - 114
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
IS - 2-3
ER -