JBC Oz Biosciences

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on February 13, 2004
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
279/7/5072    most recent
M311772200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Maxfield, A. B.
Right arrow Articles by Winge, D. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maxfield, A. B.
Right arrow Articles by Winge, D. R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print November 13, 2003
J. Biol. Chem, 10.1074/jbc.M311772200
Submitted on October 27, 2003
Revised on November 11, 2003
Accepted on November 13, 2003

Cox17 is functional when tethered to the mitochondrial inner membrane

Andrew B. Maxfield, Daren N. Heaton, and Dennis R. Winge

Department of Biochemistry and Internal Medicine, University of Utah Health Sciences Center, Salt Lake City, UT 84132-2408

Corresponding Author: dennis.winge{at}hsc.utah.edu

Cox17 is an essential protein in the assembly of cytochrome c oxidase within the mitochondrion. Cox17 is implicated in providing copper ions for formation of CuA and CuB sites in the oxidase complex. To address whether Cox17 is functional in shuttling copper ions to the mitochondrion, Cox17 was tethered to the mitochondrial inner membrane by a fusion to the transmembrane domain of the inner membrane protein, Sco2. The copper-binding domain of Sco2 that projects into the intermitochondrial membrane space (IMS) was replaced with Cox17. The Sco2/Cox17 fusion protein containing the mitochondrial import sequence and transmembrane segment of Sco2 is exclusively localized within the mitochondrion. The Sco2/Cox17 protein restores respiratory growth and normal cytochrome oxidase activity in cox17D cells. These studies suggest that Cox17’s function is confined to the mitochondrial intermembrane space. Domain mapping of yeast Cox17 reveals that the carboxyl-terminal segment of the protein has a function within the IMS that is independent of copper ion binding. The essential C-terminal function of Cox17 maps to a candidate amphipathic helix that is important for mitochondrial uptake and retention of the Cox17 protein. This motif can be spatially separated from the N-terminal copper-binding functional motif. Possible roles of the C-terminal motif are discussed.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
D. Horn, H. Al-Ali, and A. Barrientos
Cmc1p Is a Conserved Mitochondrial Twin CX9C Protein Involved in Cytochrome c Oxidase Biogenesis
Mol. Cell. Biol., July 1, 2008; 28(13): 4354 - 4364.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Rigby, P. A. Cobine, O. Khalimonchuk, and D. R. Winge
Mapping the Functional Interaction of Sco1 and Cox2 in Cytochrome Oxidase Biogenesis
J. Biol. Chem., May 30, 2008; 283(22): 15015 - 15022.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
S. Lutsenko, N. L. Barnes, M. Y. Bartee, and O. Y. Dmitriev
Function and Regulation of Human Copper-Transporting ATPases
Physiol Rev, July 1, 2007; 87(3): 1011 - 1046.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Rigby, L. Zhang, P. A. Cobine, G. N. George, and D. R. Winge
Characterization of the Cytochrome c Oxidase Assembly Factor Cox19 of Saccharomyces cerevisiae
J. Biol. Chem., April 6, 2007; 282(14): 10233 - 10242.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. A. Cobine, F. Pierrel, M. L. Bestwick, and D. R. Winge
Mitochondrial Matrix Copper Complex Used in Metallation of Cytochrome Oxidase and Superoxide Dismutase
J. Biol. Chem., December 1, 2006; 281(48): 36552 - 36559.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
L. Banci, I. Bertini, S. Ciofi-Baffoni, N. G. Kandias, N. J. Robinson, G. A. Spyroulias, X.-C. Su, S. Tottey, and M. Vanarotti
The delivery of copper for thylakoid import observed by NMR
PNAS, May 30, 2006; 103(22): 8320 - 8325.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. A. Cobine, F. Pierrel, S. C. Leary, F. Sasarman, Y.-C. Horng, E. A. Shoubridge, and D. R. Winge
The P174L Mutation in Human Sco1 Severely Compromises Cox17-dependent Metallation but Does Not Impair Copper Binding
J. Biol. Chem., May 5, 2006; 281(18): 12270 - 12276.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-C. Horng, S. C. Leary, P. A. Cobine, F. B. J. Young, G. N. George, E. A. Shoubridge, and D. R. Winge
Human Sco1 and Sco2 Function as Copper-binding Proteins
J. Biol. Chem., October 7, 2005; 280(40): 34113 - 34122.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. GenomicsHome page
H. van Bakel, E. Strengman, C. Wijmenga, and F. C. P. Holstege
Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism
Physiol Genomics, August 11, 2005; 22(3): 356 - 367.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Church, B. Goehring, D. Forsha, P. Wazny, and R. O. Poyton
A Role for Pet100p in the Assembly of Yeast Cytochrome c Oxidase: INTERACTION WITH A SUBASSEMBLY THAT ACCUMULATES IN A pet100 MUTANT
J. Biol. Chem., January 21, 2005; 280(3): 1854 - 1863.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Abajian, L. A. Yatsunyk, B. E. Ramirez, and A. C. Rosenzweig
Yeast Cox17 Solution Structure and Copper(I) Binding
J. Biol. Chem., December 17, 2004; 279(51): 53584 - 53592.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
S. C. Leary, B. A. Kaufman, G. Pellecchia, G.-H. Guercin, A. Mattman, M. Jaksch, and E. A. Shoubridge
Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase
Hum. Mol. Genet., September 1, 2004; 13(17): 1839 - 1848.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-C. Horng, P. A. Cobine, A. B. Maxfield, H. S. Carr, and D. R. Winge
Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase
J. Biol. Chem., August 20, 2004; 279(34): 35334 - 35340.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. H. Barros, A. Johnson, and A. Tzagoloff
COX23, a Homologue of COX17, Is Required for Cytochrome Oxidase Assembly
J. Biol. Chem., July 23, 2004; 279(30): 31943 - 31947.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Laliberte, L. J. Whitson, J. Beaudoin, S. P. Holloway, P. J. Hart, and S. Labbe
The Schizosaccharomyces pombe Pccs Protein Functions in Both Copper Trafficking and Metal Detoxification Pathways
J. Biol. Chem., July 2, 2004; 279(27): 28744 - 28755.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. A. Cobine, L. D. Ojeda, K. M. Rigby, and D. R. Winge
Yeast Contain a Non-proteinaceous Pool of Copper in the Mitochondrial Matrix
J. Biol. Chem., April 2, 2004; 279(14): 14447 - 14455.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.