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Published Online June 7, 2001
Science DOI: 10.1126/science.1060331

Reports

Submitted on March 1, 2001
Accepted on May 24, 2001

Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis

Caryn E. Outten 1 Thomas V. O'Halloran 2*

1 Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, USA.
2 Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, USA.

* To whom correspondence should be addressed. E-mail: t-ohalloran{at}northwestern.edu.

Intracellular zinc is thought to be available in a cytosolic pool of free or loosely-bound Zn(II) ions in the micromolar to picomolar range. To test this, we determined the mechanism of zinc sensors that control metal uptake or export in E. coli and calibrated their response against the thermodynamically-defined free zinc concentration. Whereas the cellular zinc quota is tenth millimolar, free Zn(II) concentrations that trigger transcription of zinc uptake or efflux machinery are femtomolar, or six orders of magnitude less than one atom per cell. This is not consistent with a cytosolic pool of free Zn(II) and suggests an extraordinary intracellular zinc binding capacity. Thus, cells exert tight control over cytosolic metal concentrations, even for relatively low toxicity metals such as zinc.


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A Nickel-Cobalt-sensing ArsR-SmtB Family Repressor. CONTRIBUTIONS OF CYTOSOL AND EFFECTOR BINDING SITES TO METAL SELECTIVITY.
J. S. Cavet, W. Meng, M. A. Pennella, R. J. Appelhoff, D. P. Giedroc, and N. J. Robinson (2002)
J. Biol. Chem. 277, 38441-38448
   Abstract »    Full Text »    PDF »
Surplus Zinc Is Handled by Zym1 Metallothionein and Zhf Endoplasmic Reticulum Transporter in Schizosaccharomyces pombe.
G. P. M. Borrelly, M. D. Harrison, A. K. Robinson, S. G. Cox, N. J. Robinson, and S. K. Whitehall (2002)
J. Biol. Chem. 277, 30394-30400
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Mammalian metal response element-binding transcription factor-1 functions as a zinc sensor in yeast, but not as a sensor of cadmium or oxidative stress.
P. J. Daniels, D. Bittel, I. V. Smirnova, D. R. Winge, and G. K. Andrews (2002)
Nucleic Acids Res. 30, 3130-3140
   Abstract »    Full Text »    PDF »
Substrate-activated Zinc Binding of Metallo-beta -lactamases. PHYSIOLOGICAL IMPORTANCE OF THE MONONUCLEAR ENZYMES.
S. Wommer, S. Rival, U. Heinz, M. Galleni, J.-M. Frere, N. Franceschini, G. Amicosante, B. Rasmussen, R. Bauer, and H.-W. Adolph (2002)
J. Biol. Chem. 277, 24142-24147
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A Novel Zinc-regulated Human Zinc Transporter, hZTL1, Is Localized to the Enterocyte Apical Membrane.
R. A. Cragg, G. R. Christie, S. R. Phillips, R. M. Russi, S. Kury, J. C. Mathers, P. M. Taylor, and D. Ford (2002)
J. Biol. Chem. 277, 22789-22797
   Abstract »    Full Text »    PDF »
A Transporter in the Endoplasmic Reticulum of Schizosaccharomyces pombe Cells Mediates Zinc Storage and Differentially Affects Transition Metal Tolerance.
S. Clemens, T. Bloss, C. Vess, D. Neumann, D. H. Nies, and U. zur Nieden (2002)
J. Biol. Chem. 277, 18215-18221
   Abstract »    Full Text »    PDF »


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