Document Detail


A heme-sensing mechanism in the translational regulation of mitochondrial cytochrome c oxidase biogenesis.
MedLine Citation:
PMID:  23217259     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Heme plays fundamental roles as cofactor and signaling molecule in multiple pathways devoted to oxygen sensing and utilization in aerobic organisms. For cellular respiration, heme serves as a prosthetic group in electron transfer proteins and redox enzymes. Here we report that in the yeast Saccharomyces cerevisiae, a heme-sensing mechanism translationally controls the biogenesis of cytochrome c oxidase (COX), the terminal mitochondrial respiratory chain enzyme. We show that Mss51, a COX1 mRNA-specific translational activator and Cox1 chaperone, which coordinates Cox1 synthesis in mitoribosomes with its assembly in COX, is a heme-binding protein. Mss51 contains two heme regulatory motifs or Cys-Pro-X domains located in its N terminus. Using a combination of in vitro and in vivo approaches, we have demonstrated that these motifs are important for heme binding and efficient performance of Mss51 functions. We conclude that heme sensing by Mss51 regulates COX biogenesis and aerobic energy production.
Authors:
Iliana C Soto; Flavia Fontanesi; Richard S Myers; Patrice Hamel; Antoni Barrientos
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell metabolism     Volume:  16     ISSN:  1932-7420     ISO Abbreviation:  Cell Metab.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-10     Completed Date:  2013-05-22     Revised Date:  2013-12-11    
Medline Journal Info:
Nlm Unique ID:  101233170     Medline TA:  Cell Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  801-13     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Inc. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Amino Acid Sequence
Electron Transport Complex IV / genetics,  metabolism*
Heme / metabolism*
Kinetics
Mitochondria / enzymology*
Mitochondrial Turnover
Molecular Sequence Data
Mutation
Protein Binding
Protein Processing, Post-Translational
Recombinant Proteins / biosynthesis,  chemistry,  genetics
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Sequence Alignment
Transcription Factors / genetics,  metabolism
Grant Support
ID/Acronym/Agency:
F31 GM081975/GM/NIGMS NIH HHS; GM081975/GM/NIGMS NIH HHS; P30 AI 073961/AI/NIAID NIH HHS; R01 GM071775/GM/NIGMS NIH HHS; R01 GM071775-06/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Mss51 protein, S cerevisiae; 0/Recombinant Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors; 42VZT0U6YR/Heme; EC 1.9.3.1/Cox1 protein, S cerevisiae; EC 1.9.3.1/Electron Transport Complex IV
Comments/Corrections

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