PMID- 22219186
OWN - NLM
STAT- MEDLINE
DCOM- 20120424
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 287
IP  - 10
DP  - 2012 Mar 2
TI  - Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome 
      oxidase in assembly mutants.
PG  - 7289-300
LID - 10.1074/jbc.M111.313148 [doi]
AB  - Stalled biogenesis of the mitochondrial cytochrome c oxidase (CcO) complex 
      results in degradation of subunits containing redox cofactors. The conserved Oma1 
      metalloproteinase mediates facile Cox1 degradation in cells lacking the Coa2 
      assembly factor, but not in a series of other mutants stalled in CcO maturation. 
      Oma1 is activated in coa2Delta cells, but the selective Cox1 degradation does not 
      arise merely from its activation. Oma1 is also active in cells with dysfunctional 
      mitochondria and cox11Delta cells impaired in CcO maturation, but this activation 
      does not result in Oma1-mediated Cox1 degradation. The facile and selective 
      degradation of Cox1 in coa2Delta cells, relative to other CcO assembly mutants, is 
      likely due to impaired hemylation and subsequent misfolding of the subunit. 
      Specific Cox1 proteolysis in coa2Delta cells arises from a combination of Oma1 
      activation and a susceptible conformation of Cox1.
FAU - Khalimonchuk, Oleh
AU  - Khalimonchuk O
AD  - Department of Medicine and Biochemistry, University of Utah Health Sciences 
      Center, Salt Lake City, Utah 84132, USA.
FAU - Jeong, Mi-Young
AU  - Jeong MY
FAU - Watts, Talina
AU  - Watts T
FAU - Ferris, Elliott
AU  - Ferris E
FAU - Winge, Dennis R
AU  - Winge DR
LA  - eng
GR  - R01 ES003817/ES/NIEHS NIH HHS/United States
GR  - R37 ES003817/ES/NIEHS NIH HHS/United States
GR  - ES03817/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20120104
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Coa2 protein, S cerevisiae)
RN  - 0 (Membrane Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 1.9.3.1 (Cox1 protein, S cerevisiae)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - EC 3.4.- (Metalloproteases)
RN  - EC 3.4.- (Oma1 protein, S cerevisiae)
SB  - IM
MH  - Electron Transport Complex IV/genetics/*metabolism
MH  - Enzyme Activation/physiology
MH  - Membrane Proteins/genetics/metabolism
MH  - Metalloproteases/genetics/*metabolism
MH  - Mitochondria/*enzymology/genetics
MH  - Mutation
MH  - *Proteolysis
MH  - Saccharomyces cerevisiae/*enzymology/genetics
MH  - Saccharomyces cerevisiae Proteins/genetics/*metabolism
PMC - PMC3293553
EDAT- 2012/01/06 06:00
MHDA- 2012/04/25 06:00
PMCR- 2013/03/02
CRDT- 2012/01/06 06:00
PHST- 2012/01/06 06:00 [entrez]
PHST- 2012/01/06 06:00 [pubmed]
PHST- 2012/04/25 06:00 [medline]
PHST- 2013/03/02 00:00 [pmc-release]
AID - S0021-9258(20)61044-4 [pii]
AID - M111.313148 [pii]
AID - 10.1074/jbc.M111.313148 [doi]
PST - ppublish
SO  - J Biol Chem. 2012 Mar 2;287(10):7289-300. doi: 10.1074/jbc.M111.313148. Epub 2012 
      Jan 4.