Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro

BioMetals

Volumn 28, Issue 3, 2015, Pages 577-585

  Petzoldt, Svenja ^a,b   Kahra, Dana ^a   Kovermann, Michael ^a   Dingeldein, Artur P G ^a   Niemiec, Moritz S ^a   Ådén, Jörgen ^a   Wittung Stafshede, Pernilla ^a  

^a UMEÅ UNIVERSITY   (Sweden)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Atox1; Copper chaperone for superoxide dismutase (SOD); Human copper transport; Proton NMR; Size exclusion chromatography

Indexed keywords

ATOX1 PROTEIN, HUMAN; CCS PROTEIN, HUMAN; CHAPERONE; COPPER; METALLOCHAPERONE; PROTEIN BINDING;

CYTOPLASM; HUMAN; METABOLISM; SIZE EXCLUSION CHROMATOGRAPHY;

CHROMATOGRAPHY, GEL; COPPER; CYTOPLASM; HUMANS; METALLOCHAPERONES; MOLECULAR CHAPERONES; PROTEIN BINDING;

EID: 84939961295     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-015-9832-1     Document Type: Article

References (30)

1. Achila D, Banci L, Bertini I, Bunce J, Ciofi-Baffoni S, Huffman DL (2006) Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake. Proc Natl Acad Sci USA 103(15):5729-5734
2. Allen S, Badarau A, Dennison C (2012) Cu(I) affinities of the domain 1 and 3 sites in the human metallochaperone for Cu, Zn-superoxide dismutase. Biochemistry 51(7):1439-1448
3. Arnesano F, Banci L, Bertini I, Ciofi-Baffoni S, Molteni E, Huffman DL, O'Halloran TV (2002) Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res 12(2):255-271
4. Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A (2005) An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein. FEBS J 272(3):865-871
5. Banci L, Bertini I, Cantini F, Rosenzweig AC, Yatsunyk LA (2008) Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1. Biochemistry 47(28):7423-7429
6. Banci L, Bertini I, Cantini F, Massagni C, Migliardi M, Rosato A (2009) An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1. J Biol Chem 284(14):9354-9360
7. Banci L, Bertini I, Cantini F, Kozyreva T, Massagni C, Palumaa P, Rubino JT, Zovo K (2012) Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). Proc Natl Acad Sci USA 109(34):13555-13560
8. Banci L, Cantini F, Kozyreva T, Rubino JT (2013) Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants. ChemBioChem 14(14):1839-1844
9. Berger S, Braun S (2004) 200 and more NMR experiments. A practical course. Wiley-VHC, Weinheim
10. Boal AK, Rosenzweig AC (2009) Structural biology of copper trafficking. Chem Rev 109(10):4760-4779
11. Festa RA, Thiele DJ (2011) Copper: an essential metal in biology. Curr Biol 21(21):R877-R883
12. Harris ED (2003) Basic and clinical aspects of copper. Crit Rev Clin Lab Sci 40(5):547-586
13. Harrison MD, Jones CE, Dameron CT (1999) Copper chaperones: function, structure and copper-binding properties. J Biol Inorg Chem 4(2):145-153
14. Hatori Y, Lutsenko S (2013) An expanding range of functions for the copper chaperone/antioxidant protein Atox1. Antioxid Redox Signal 19:945-957
15. Huffman DL, O'Halloran TV (2001) Function, structure, and mechanism of intracellular copper trafficking proteins. Annu Rev Biochem 70:677-701
16. Jones JA, Wilkins DK, Smith LJ, Dobson CM (1997) Characterization of protein unfolding by NMR diffusion measurements. J Biomol NMR 10:199-203
17. Kim BE, Nevitt T, Thiele DJ (2008) Mechanisms for copper acquisition, distribution and regulation. Nat Chem Biol 4(3):176-185
18. Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol 8(9):751-755
19. Maryon EB, Molloy SA, Kaplan JH (2013) Cellular glutathione plays a key role in copper uptake mediated by human copper transporter 1. Am J Physiol Cell Physiol 304(8):C768-C779
20. Niemiec MS, Weise CF, Wittung-Stafshede P (2012) In vitro thermodynamic dissection of human copper transfer from chaperone to target protein. PLoS One 7(5):e36102
21. Niemiec MS, Dingeldein AP, Wittung-Stafshede P (2014) T versus D in the MTCXXC motif of copper transport proteins plays a role in directional metal transport. J Biol Inorg Chem 19:1037-1047
22. Nilsson L, Aden J, Niemiec MS, Nam K, Wittung-Stafshede P (2013) Small pH and salt variations radically alter the thermal stability of metal-binding domains in the copper transporter, Wilson disease protein. J Phys Chem B 117(42):13038-13050
23. O'Halloran TV, Culotta VC (2000) Metallochaperones, an intracellular shuttle service for metal ions. J Biol Chem 275(33):25057-25060
24. Ohrvik H, Thiele DJ (2014) How copper traverses cellular membranes through the mammalian copper transporter 1, Ctr1. Ann N Y Acad Sci 1314:32-41
25. Pope CR, De Feo CJ, Unger VM (2013) Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes. Proc Natl Acad Sci USA 110(51):20491-20496
26. Puig S, Thiele DJ (2002) Molecular mechanisms of copper uptake and distribution. Curr Opin Chem Biol 6(2):171-180
27. Robinson NJ, Winge DR (2010) Copper metallochaperones. Annu Rev Biochem 79:537-562
28. Tanner JE (1970) Use of the stimulated echo in nmr diffusion studies. J Chem Phys 52(5):2523-2526
29. Wong PC, Waggoner D, Subramaniam JR, Tessarollo L, Bartnikas TB, Culotta VC, Price DL, Rothstein J, Gitlin JD (2000) Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc Natl Acad Sci USA 97(6):2886-2891
30. Xiao Z, Wedd AG (2002) A C-terminal domain of the membrane copper pump Ctr1 exchanges copper(I) with the copper chaperone Atx1. Chem Commun (Camb) 6:588-589