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Science 31 October 1997:
Vol. 278. no. 5339, pp. 853 - 856
DOI: 10.1126/science.278.5339.853
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Reports

Metal Ion Chaperone Function of the Soluble Cu(I) Receptor Atx1

R. A. Pufahl, C. P. Singer, K. L. Peariso, S.-J. Lin, P. J. Schmidt, C. J. Fahrni, V. Cizewski Culotta, J. E. Penner-Hahn, T. V. O'Halloran *

Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.

R. A. Pufahl, C. P. Singer, C. J. Fahrni, T. V. O'Halloran, Department of Chemistry and Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
K. L. Peariso and J. E. Penner-Hahn, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
S.-J. Lin, P. J. Schmidt, V. Cizewski Culotta, Department of Environmental Health Sciences, Johns Hopkins University, Baltimore, MD 21205, USA.
*   To whom correspondence should be addressed. E-mail: t-ohalloran{at}nwu.edu

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Role of the Copper-binding Domain in the Copper Transport Function of ATP7B, the P-type ATPase Defective in Wilson Disease.
J. R. Forbes, G. Hsi, and D. W. Cox (1999)
J. Biol. Chem. 274, 12408-12413
   Abstract »    Full Text »    PDF »
Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase.
T. D. Rae, P. J. Schmidt, R. A. Pufahl, V. C. Culotta, and T. V. O'Halloran (1999)
Science 284, 805-808
   Abstract »    Full Text »
Metallothionein Is Part of a Zinc-scavenging Mechanism for Cell Survival under Conditions of Extreme Zinc Deprivation.
D. A. Suhy, K. D. Simon, D. I. H. Linzer, and T. V. O'Halloran (1999)
J. Biol. Chem. 274, 9183-9192
   Abstract »    Full Text »    PDF »
IV. Wilson's disease and Menkes disease.
M. Schaefer and J. D. Gitlin (1999)
Am J Physiol Gastrointest Liver Physiol 276, G311-G314
   Abstract »    Full Text »    PDF »
Coordination of Zn2+ (and Cd2+) by Prokaryotic Metallothionein. INVOLVEMENT OF HIS-IMIDAZOLE.
M. J. Daniels, J. S. Turner-Cavet, R. Selkirk, H. Sun, J. A. Parkinson, P. J. Sadler, and N. J. Robinson (1998)
J. Biol. Chem. 273, 22957-22961
   Abstract »    Full Text »    PDF »
An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter.
C. Thelwell, N. J. Robinson, and J. S. Turner-Cavet (1998)
PNAS 95, 10728-10733
   Abstract »    Full Text »    PDF »
Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis.
E. Himelblau, H. Mira, S.-J. Lin, V. Cizewski Culotta, L. Peñarrubia, and R. M. Amasino (1998)
Plant Physiology 117, 1227-1234
   Abstract »    Full Text »
Energetics of Copper Trafficking between the Atx1 Metallochaperone and the Intracellular Copper Transporter, Ccc2.
D. L. Huffman and T. V. O'Halloran (2000)
J. Biol. Chem. 275, 18611-18614
   Abstract »    Full Text »    PDF »
Characterization of the Saccharomyces cerevisiae High Affinity Copper Transporter Ctr3.
M. M. O. Pena, S. Puig, and D. J. Thiele (2000)
J. Biol. Chem. 275, 33244-33251
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Mitochondrial Control of Iron Homeostasis. A GENOME WIDE ANALYSIS OF GENE EXPRESSION IN A YEAST FRATAXIN-DEFICIENT STRAIN.
F. Foury and D. Talibi (2001)
J. Biol. Chem. 276, 7762-7768
   Abstract »    Full Text »    PDF »
Copper Activation of Superoxide Dismutase 1 (SOD1) in Vivo. ROLE FOR PROTEIN-PROTEIN INTERACTIONS WITH THE COPPER CHAPERONE FOR SOD1.
P. J. Schmidt, C. Kunst, and V. C. Culotta (2000)
J. Biol. Chem. 275, 33771-33776
   Abstract »    Full Text »    PDF »
Mutational Analysis of the Mitochondrial Copper Metallochaperone Cox17.
D. Heaton, T. Nittis, C. Srinivasan, and D. R. Winge (2000)
J. Biol. Chem. 275, 37582-37587
   Abstract »    Full Text »    PDF »


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