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Science 30 April 1999:
Vol. 284. no. 5415, pp. 805 - 808
DOI: 10.1126/science.284.5415.805
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Reports

Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase

T. D. Rae, 1 P. J. Schmidt, 3 R. A. Pufahl, 1 V. C. Culotta, 3* T. V. O'Halloran 12*

The copper chaperone for the superoxide dismutase (CCS) gene is necessary for expression of an active, copper-bound form of superoxide dismutase (SOD1) in vivo in spite of the high affinity of SOD1 for copper (dissociation constant = 6 fM) and the high intracellular concentrations of both SOD1 (10 µM in yeast) and copper (70 µM in yeast). In vitro studies demonstrated that purified Cu(I)-yCCS protein is sufficient for direct copper activation of apo-ySOD1 but is necessary only when the concentration of free copper ions ([Cu]free) is strictly limited. Moreover, the physiological requirement for yCCS in vivo was readily bypassed by elevated copper concentrations and abrogation of intracellular copper-scavenging systems such as the metallothioneins. This metallochaperone protein activates the target enzyme through direct insertion of the copper cofactor and apparently functions to protect the metal ion from binding to intracellular copper scavengers. These results indicate that intracellular [Cu]free is limited to less than one free copper ion per cell and suggest that a pool of free copper ions is not used in physiological activation of metalloenzymes.

1 Department of Chemistry and
2 Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
3 Department of Environmental Health Sciences, The Johns Hopkins University, Baltimore, MD 21205, USA.
*   To whom correspondence should be addressed. E-mail: vculotta{at}jhsph.edu; t-ohalloran{at}nwu.edu

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   Abstract »    Full Text »    PDF »
A Cadmium-Lead-sensing ArsR-SmtB Repressor with Novel Sensory Sites: COMPLEMENTARY METAL DISCRIMINATION BY NMTR AND CMTR IN A COMMON CYTOSOL.
J. S. Cavet, A. I. Graham, W. Meng, and N. J. Robinson (2003)
J. Biol. Chem. 278, 44560-44566
   Abstract »    Full Text »    PDF »
Prion, Amyloid {beta}-derived Cu(II) Ions, or Free Zn(II) Ions Support S-Nitroso-dependent Autocleavage of Glypican-1 Heparan Sulfate.
K. Mani, F. Cheng, B. Havsmark, M. Jonsson, M. Belting, and L.-A. Fransson (2003)
J. Biol. Chem. 278, 38956-38965
   Abstract »    Full Text »    PDF »
Copper Modulates the Degradation of Copper Chaperone for Cu,Zn Superoxide Dismutase by the 26 S Proteosome.
J. Bertinato and M. R. L'Abbe (2003)
J. Biol. Chem. 278, 35071-35078
   Abstract »    Full Text »    PDF »
From The Cover: Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family.
E. Luk, M. Carroll, M. Baker, and V. C. Culotta (2003)
PNAS 100, 10353-10357
   Abstract »    Full Text »    PDF »
Mechanisms of Biosynthesis of Mammalian Copper/Zinc Superoxide Dismutase.
T. B. Bartnikas and J. D. Gitlin (2003)
J. Biol. Chem. 278, 33602-33608
   Abstract »    Full Text »    PDF »
S-Nitrosylation Signaling in Cell Biology.
B. M. Gaston, J. Carver, A. Doctor, and L. A. Palmer (2003)
Mol. Interv. 3, 253-263
   Abstract »    Full Text »    PDF »
The Copper Export Pump ATP7B Modulates the Cellular Pharmacology of Carboplatin in Ovarian Carcinoma Cells.
K. Katano, R. Safaei, G. Samimi, A. Holzer, M. Rochdi, and S. B. Howell (2003)
Mol. Pharmacol. 64, 466-473
   Abstract »    Full Text »    PDF »
Factors Controlling the Uptake of Yeast Copper/Zinc Superoxide Dismutase into Mitochondria.
L. S. Field, Y. Furukawa, T. V. O'Halloran, and V. C. Culotta (2003)
J. Biol. Chem. 278, 28052-28059
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X-ray Absorption Spectroscopy of the Copper Chaperone HAH1 Reveals a Linear Two-coordinate Cu(I) Center Capable of Adduct Formation with Exogenous Thiols and Phosphines.
M. Ralle, S. Lutsenko, and N. J. Blackburn (2003)
J. Biol. Chem. 278, 23163-23170
   Abstract »    Full Text »    PDF »
Putative functions of PrPC.
C. I. Lasmezas (2003)
Br. Med. Bull. 66, 61-70
   Abstract »    Full Text »    PDF »
Role of Nicotianamine in the Intracellular Delivery of Metals and Plant Reproductive Development.
M. Takahashi, Y. Terada, I. Nakai, H. Nakanishi, E. Yoshimura, S. Mori, and N. K. Nishizawa (2003)
PLANT CELL 15, 1263-1280
   Abstract »    Full Text »
PAA1, a P-Type ATPase of Arabidopsis, Functions in Copper Transport in Chloroplasts.
T. Shikanai, P. Muller-Moule, Y. Munekage, K. K. Niyogi, and M. Pilon (2003)
PLANT CELL 15, 1333-1346
   Abstract »    Full Text »
The mechanism of ferrichrome transport through Arn1p and its metabolism in Saccharomyces cerevisiae.
R. E. Moore, Y. Kim, and C. C. Philpott (2003)
PNAS 100, 5664-5669
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Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors.
L. A. Finney and T. V. O'Halloran (2003)
Science 300, 931-936
   Abstract »    Full Text »    PDF »
Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain. A REGULATOR OF NEURONAL COPPER HOMEOSTASIS.
K. J. Barnham, W. J. McKinstry, G. Multhaup, D. Galatis, C. J. Morton, C. C. Curtain, N. A. Williamson, A. R. White, M. G. Hinds, R. S. Norton, et al. (2003)
J. Biol. Chem. 278, 17401-17407
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