Document Detail


Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly.
MedLine Citation:
PMID:  17882260     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The assembly of cytochrome c oxidase (CcO) in yeast mitochondria is shown to be dependent on a new assembly factor designated Coa1 that associates with the mitochondrial inner membrane. Translation of the mitochondrial-encoded subunits of CcO occurs normally in coa1Delta cells, but these subunits fail to accumulate. The respiratory defect in coa1Delta cells is suppressed by high-copy MSS51, MDJ1 and COX10. Mss51 functions in Cox1 translation and elongation, whereas Cox10 participates in the biosynthesis of heme a, a key cofactor of CcO. Respiration in coa1Delta and shy1Delta cells is enhanced when Mss51 and Cox10 are coexpressed. Shy1 has been implicated in formation of the heme a3-Cu(B) site in Cox1. The interaction between Coa1 and Cox1, and the physical and genetic interactions between Coa1 and Mss51, Shy1 and Cox14 suggest that Coa1 coordinates the transition of newly synthesized Cox1 from the Mss51:Cox14 complex to the heme a cofactor insertion involving Shy1. coa1Delta cells also display a mitochondrial copper defect suggesting that Coa1 may have a direct link to copper metallation of CcO.
Authors:
Fabien Pierrel; Megan L Bestwick; Paul A Cobine; Oleh Khalimonchuk; Julia A Cricco; Dennis R Winge
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-09-20
Journal Detail:
Title:  The EMBO journal     Volume:  26     ISSN:  1460-2075     ISO Abbreviation:  EMBO J.     Publication Date:  2007 Oct 
Date Detail:
Created Date:  2007-10-17     Completed Date:  2007-12-11     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  4335-46     Citation Subset:  IM    
Affiliation:
Department of Medicine, University of Utah Health Sciences Center, University of Utah, Salt Lake City, UT 84132, USA.
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MeSH Terms
Descriptor/Qualifier:
Copper / chemistry
Electron Transport Complex IV / chemistry,  physiology*
Fungal Proteins / physiology*
Gene Expression Regulation, Fungal*
Heme / chemistry
Membrane Proteins / physiology
Mitochondria / metabolism
Mitochondrial Proteins
Models, Biological
Nuclear Proteins / physiology
Oxygen Consumption
Protein Binding
Protein Biosynthesis
Protein Processing, Post-Translational*
Saccharomyces cerevisiae Proteins / physiology*
Transcription Factors / physiology*
Grant Support
ID/Acronym/Agency:
DK P30 072437/DK/NIDDK NIH HHS; ES 03817/ES/NIEHS NIH HHS
Chemical
Reg. No./Substance:
0/COX14 protein, S cerevisiae; 0/Fungal Proteins; 0/Membrane Proteins; 0/Mitochondrial Proteins; 0/Mss51 protein, S cerevisiae; 0/Nuclear Proteins; 0/SHY1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors; 14875-96-8/Heme; 7440-50-8/Copper; EC 1.9.3.1/Electron Transport Complex IV
Comments/Corrections

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