PMID- 14729672
OWN - NLM
STAT- MEDLINE
DCOM- 20040511
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 279
IP  - 14
DP  - 2004 Apr 2
TI  - Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix.
PG  - 14447-55
AB  - The yeast mitochondrion is shown to contain a pool of copper that is distinct 
      from that associated with the two known mitochondrial cuproenzymes, superoxide 
      dismutase (Sod1) and cytochrome c oxidase (CcO) and the copper-binding CcO 
      assembly proteins Cox11, Cox17, and Sco1. Only a small fraction of mitochondrial 
      copper is associated with these cuproproteins. The bulk of the remainder is 
      localized within the matrix as a soluble, anionic, low molecular weight complex. 
      The identity of the matrix copper ligand is unknown, but the bulk of the matrix 
      copper fraction is not protein-bound. The mitochondrial copper pool is dynamic, 
      responding to changes in the cytosolic copper level. The addition of copper salts 
      to the growth medium leads to an increase in mitochondrial copper, yet the 
      expansion of this matrix pool does not induce any respiration defects. The matrix 
      copper pool is accessible to a heterologous cuproenzyme. Co-localization of human 
      Sod1 and the metallochaperone CCS within the mitochondrial matrix results in 
      suppression of growth defects of sod2Delta cells. However, in the absence of CCS 
      within the matrix, the activation of human Sod1 can be achieved by the addition 
      of copper salts to the growth medium.
FAU - Cobine, Paul A
AU  - Cobine PA
AD  - University of Utah Health Sciences Center, Salt Lake City, Utah 84132, USA.
FAU - Ojeda, Luis D
AU  - Ojeda LD
FAU - Rigby, Kevin M
AU  - Rigby KM
FAU - Winge, Dennis R
AU  - Winge DR
LA  - eng
GR  - 5P30-CA 42014/CA/NCI NIH HHS/United States
GR  - ES03817/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20040116
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (COX17 protein, S cerevisiae)
RN  - 0 (COX17 protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cation Transport Proteins)
RN  - 0 (Copper Transport Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (SOD1 protein, human)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 789U1901C5 (Copper)
RN  - EC 1.15.1.1 (Superoxide Dismutase)
RN  - EC 1.15.1.1 (Superoxide Dismutase-1)
RN  - EC 1.15.1.1 (superoxide dismutase 2)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Carrier Proteins
MH  - Cation Transport Proteins/metabolism
MH  - Copper/*metabolism
MH  - Copper Transport Proteins
MH  - Electron Transport Complex IV/metabolism
MH  - Mitochondria/*metabolism
MH  - Molecular Chaperones
MH  - Saccharomyces cerevisiae/*metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Superoxide Dismutase/metabolism
MH  - Superoxide Dismutase-1
EDAT- 2004/01/20 05:00
MHDA- 2004/05/12 05:00
CRDT- 2004/01/20 05:00
PHST- 2004/01/20 05:00 [pubmed]
PHST- 2004/05/12 05:00 [medline]
PHST- 2004/01/20 05:00 [entrez]
AID - S0021-9258(19)64121-9 [pii]
AID - 10.1074/jbc.M312693200 [doi]
PST - ppublish
SO  - J Biol Chem. 2004 Apr 2;279(14):14447-55. doi: 10.1074/jbc.M312693200. Epub 2004 
      Jan 16.