PMID- 20398622
OWN - NLM
STAT- MEDLINE
DCOM- 20110110
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1797
IP  - 6-7
DP  - 2010 Jun-Jul
TI  - Assembly factors and ATP-dependent proteases in cytochrome c oxidase biogenesis.
PG  - 1149-58
LID - 10.1016/j.bbabio.2010.04.006 [doi]
AB  - Eukaryotic cytochrome c oxidase (CcO), the terminal enzyme of the 
      energy-transducing mitochondrial electron transport chain is a hetero-oligomeric, 
      heme-copper oxidase complex composed of both mitochondrially and nuclear-encoded 
      subunits. It is embedded in the inner mitochondrial membrane where it couples the 
      transfer of electrons from reduced cytochrome c to molecular oxygen with 
      vectorial proton translocation across the membrane. The biogenesis of CcO is a 
      complicated sequential process that requires numerous specific accessory 
      proteins, so-called assembly factors, which include translational activators, 
      translocases, molecular chaperones, copper metallochaperones and heme a 
      biosynthetic enzymes. Besides these CcO-specific protein factors, the correct 
      biogenesis of CcO requires an even greater number of proteins with much broader 
      substrate specificities. Indeed, growing evidence indicates that mitochondrial 
      ATP-dependent proteases might play an important role in CcO biogenesis. Out of 
      the four identified energy-dependent mitochondrial proteases, three were shown to 
      be directly involved in proteolysis of CcO subunits. In addition to their 
      well-established protein-quality control function these oligomeric proteolytic 
      complexes with chaperone-like activities may function as molecular chaperones 
      promoting productive folding and assembly of subunit proteins. In this review, we 
      summarize the current knowledge of the functional involvement of eukaryotic 
      CcO-specific assembly factors and highlight the possible significance for CcO 
      biogenesis of mitochondrial ATP-dependent proteases.
CI  - Copyright (c) 2010 Elsevier B.V. All rights reserved.
FAU - Stiburek, Lukas
AU  - Stiburek L
AD  - Charles University in Prague, First Faculty of Medicine, Department of 
      Pediatrics, Prague, Czech Republic. Lukas.Stiburek@lf1.cuni.cz
FAU - Zeman, Jiri
AU  - Zeman J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20100414
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Molecular Chaperones)
RN  - 0 (Protein Subunits)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - EC 3.4.21.- (ATP-Dependent Proteases)
SB  - IM
MH  - ATP-Dependent Proteases/*metabolism
MH  - Animals
MH  - Electron Transport Complex IV/*biosynthesis/chemistry
MH  - Humans
MH  - Mitochondria/metabolism
MH  - Models, Biological
MH  - Molecular Chaperones/*metabolism
MH  - Protein Subunits
MH  - Saccharomyces cerevisiae/metabolism
EDAT- 2010/04/20 06:00
MHDA- 2011/01/11 06:00
CRDT- 2010/04/20 06:00
PHST- 2009/11/04 00:00 [received]
PHST- 2010/03/14 00:00 [revised]
PHST- 2010/04/07 00:00 [accepted]
PHST- 2010/04/20 06:00 [entrez]
PHST- 2010/04/20 06:00 [pubmed]
PHST- 2011/01/11 06:00 [medline]
AID - S0005-2728(10)00139-8 [pii]
AID - 10.1016/j.bbabio.2010.04.006 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2010 Jun-Jul;1797(6-7):1149-58. doi: 
      10.1016/j.bbabio.2010.04.006. Epub 2010 Apr 14.