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Article ; Online: Repeated Low-level Red-light Therapy: The Next Wave in Myopia Management?

Salzano, Aaron D / Khanal, Safal / Cheung, Nathan L / Weise, Katherine K / Jenewein, Erin C / Horn, Darryl M / Mutti, Donald O / Gawne, Timothy J

Optometry and vision science : official publication of the American Academy of Optometry

2023 Volume 100, Issue 12, Page(s) 812–822

Abstract: Significance: Exposure to long-wavelength light has been proposed as a potential intervention to slow myopia progression in children. This article provides an evidence-based review of the safety and myopia control efficacy of red light and discusses the ...

Abstract	Significance: Exposure to long-wavelength light has been proposed as a potential intervention to slow myopia progression in children. This article provides an evidence-based review of the safety and myopia control efficacy of red light and discusses the potential mechanisms by which red light may work to slow childhood myopia progression.The spectral composition of the ambient light in the visual environment has powerful effects on eye growth and refractive development. Studies in mammalian and primate animal models (macaque monkeys and tree shrews) have shown that daily exposure to long-wavelength (red or amber) light promotes slower eye growth and hyperopia development and inhibits myopia induced by form deprivation or minus lens wear. Consistent with these results, several recent randomized controlled clinical trials in Chinese children have demonstrated that exposure to red light for 3 minutes twice a day significantly reduces myopia progression and axial elongation. These findings have collectively provided strong evidence for the potential of using red light as a myopia control intervention in clinical practice. However, several questions remain unanswered. In this article, we review the current evidence on the safety and efficacy of red light as a myopia control intervention, describe potential mechanisms, and discuss some key unresolved issues that require consideration before red light can be broadly translated into myopia control in children.
MeSH term(s)	Animals ; Child ; Humans ; Eye ; Myopia/prevention & control ; Refraction, Ocular ; Hyperopia ; Tupaiidae ; Phototherapy
Language	English
Publishing date	2023-10-25
Publishing country	United States
Document type	Review ; Journal Article
ZDB-ID	1001706-9
ISSN	1538-9235 ; 1040-5488
ISSN (online)	1538-9235
ISSN	1040-5488
DOI	10.1097/OPX.0000000000002083
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Article ; Online: Mitochondrial copper metabolism and delivery to cytochrome c oxidase.

Horn, Darryl / Barrientos, Antoni

IUBMB life

2008 Volume 60, Issue 7, Page(s) 421–429

Abstract: Metals are essential elements of all living organisms. Among them, copper is required for a multiplicity of functions including mitochondrial oxidative phosphorylation and protection against oxidative stress. Here we will focus on describing the pathways ...

Abstract	Metals are essential elements of all living organisms. Among them, copper is required for a multiplicity of functions including mitochondrial oxidative phosphorylation and protection against oxidative stress. Here we will focus on describing the pathways involved in the delivery of copper to cytochrome c oxidase (COX), a mitochondrial metalloenzyme acting as the terminal enzyme of the mitochondrial respiratory chain. The catalytic core of COX is formed by three mitochondrially-encoded subunits and contains three copper atoms. Two copper atoms bound to subunit 2 constitute the Cu(A) site, the primary acceptor of electrons from ferrocytochrome c. The third copper, Cu(B), is associated with the high-spin heme a(3) group of subunit 1. Recent studies, mostly performed in the yeast Saccharomyces cerevisiae, have provided new clues about 1) the source of the copper used for COX metallation; 2) the roles of Sco1p and Cox11p, the proteins involved in the direct delivery of copper to the Cu(A) and Cu(B) sites, respectively; 3) the action mechanism of Cox17p, a copper chaperone that provides copper to Sco1p and Cox11p; 4) the existence of at least four Cox17p homologues carrying a similar twin CX(9)C domain suggestive of metal binding, Cox19p, Cox23p, Pet191p and Cmc1p, that could be part of the same pathway; and 5) the presence of a disulfide relay system in the intermembrane space of mitochondria that mediates import of proteins with conserved cysteines motifs such as the CX(9)C characteristic of Cox17p and its homologues. The different pathways are reviewed and discussed in the context of both mitochondrial COX assembly and copper homeostasis.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Binding Sites ; Copper/metabolism ; Electron Transport Complex IV/metabolism ; Gene Expression Regulation ; Gene Expression Regulation, Fungal ; Homeostasis ; Humans ; Ions ; Ligands ; Mitochondria/metabolism ; Models, Biological ; Saccharomyces cerevisiae
Chemical Substances	Ions ; Ligands ; Copper (789U1901C5) ; Adenosine Triphosphate (8L70Q75FXE) ; Electron Transport Complex IV (EC 1.9.3.1)
Language	English
Publishing date	2008-05-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1492141-8
ISSN	1521-6551 ; 1521-6543
ISSN (online)	1521-6551
ISSN	1521-6543
DOI	10.1002/iub.50
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Article ; Online: Rcl1 protein, a novel nuclease for 18 S ribosomal RNA production.

Horn, Darryl M / Mason, Saundra L / Karbstein, Katrin

The Journal of biological chemistry

2011 Volume 286, Issue 39, Page(s) 34082–34087

Abstract: In all forms of life, rRNAs for the small and large ribosomal subunit are co-transcribed as a single transcript. Although this ensures the equimolar production of rRNAs, it requires the endonucleolytic separation of pre-rRNAs to initiate rRNA production. ...

Abstract	In all forms of life, rRNAs for the small and large ribosomal subunit are co-transcribed as a single transcript. Although this ensures the equimolar production of rRNAs, it requires the endonucleolytic separation of pre-rRNAs to initiate rRNA production. In yeast, processing of the primary transcript encoding 18 S, 5.8 S, and 25 S rRNAs has been studied extensively. Nevertheless, most nucleases remain to be identified. Here, we show that Rcl1, conserved in all eukaryotes, cleaves pre-rRNA at so-called site A(2), a co-transcriptional cleavage step that separates rRNAs destined for the small and large subunit. Recombinant Rcl1 cleaves pre-rRNA mimics at site A(2) in a reaction that is sensitive to nearby RNA mutations that inhibit cleavage in vivo. Furthermore, mutations in Rcl1 disrupt rRNA processing at site A(2) in vivo and in vitro. Together, these results demonstrate that the role of Rcl1 in eukaryotic pre-rRNA processing is identical to that of RNase III in bacteria: to co-transcriptionally separate the pre-rRNAs destined for the small and large subunit. Furthermore, because Rcl1 has no homology to other known endonucleases, these data also establish a novel class of nucleases.
MeSH term(s)	Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; RNA Precursors/genetics ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional/physiology ; RNA, Fungal/genetics ; RNA, Fungal/metabolism ; RNA, Ribosomal, 18S/genetics ; RNA, Ribosomal, 18S/metabolism ; Ribonucleases/genetics ; Ribonucleases/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Nuclear Proteins ; RCL1 protein, S cerevisiae ; RNA Precursors ; RNA, Fungal ; RNA, Ribosomal, 18S ; Saccharomyces cerevisiae Proteins ; Ribonucleases (EC 3.1.-)
Language	English
Publishing date	2011-08-17
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.268649
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Article ; Online: Comparison of LC-MS-MS and GC-MS Analysis of Benzodiazepine Compounds Included in the Drug Demand Reduction Urinalysis Program.

Perez, Erick Roman / Knapp, Joshua A / Horn, Carl K / Stillman, Stedra L / Evans, James E / Arfsten, Darryl P

Journal of analytical toxicology

2016 Volume 40, Issue 3, Page(s) 201–207

Abstract: Liquid chromatography-tandem mass spectrometry (LC-MS-MS) offers specific advantages over gas chromatography-mass spectrometry (GC-MS) such as the ability to identify and measure a broader range of compounds with minimal sample preparation. Comparative ... ...

Abstract	Liquid chromatography-tandem mass spectrometry (LC-MS-MS) offers specific advantages over gas chromatography-mass spectrometry (GC-MS) such as the ability to identify and measure a broader range of compounds with minimal sample preparation. Comparative analysis of LC-MS-MS versus GC-MS was performed for urinalysis detection of five benzodiazepine compounds currently part of the Department of Defense (DoD) Drug Demand Reduction Program (DDRP) testing panel; alpha-hydroxyalprazolam, oxazepam, lorazepam, nordiazepam and temazepam. In the analyses of internally prepared control urine samples at concentrations around the DDRP administrative decision point for benzodiazepines (100 ng/mL), both technologies produced comparable results with average accuracies between 99.7 and 107.3% and average coefficients of variation (%CV) <9%. Analysis of service member specimens that screened positive for benzodiazepines using both technologies produced comparable results for all analytes. Different degrees of matrix effect were observed for all analytes in the LC-MS-MS analysis. However, the effects were controlled by using deuterated internal standards (ISTDs). Additionally, there was a 39% increase in nordiazepam mean concentration analyzed by LC-MS-MS due to suppression of the ISTD ion by the flurazepam metabolite 2-hydroxyethylflurazepam. The ease and speed of sample extraction, the broader range of compounds that can be analyzed and shorter run time make the LC-MS-MS technology a suitable and expedient alternative confirmation technology for benzodiazepine testing.
MeSH term(s)	Benzodiazepines/urine ; Chromatography, Liquid/methods ; Gas Chromatography-Mass Spectrometry/methods ; Humans ; Limit of Detection ; Tandem Mass Spectrometry/methods
Chemical Substances	Benzodiazepines (12794-10-4)
Language	English
Publishing date	2016-04
Publishing country	England
Document type	Comparative Study ; Journal Article
ZDB-ID	752391-9
ISSN	1945-2403 ; 0146-4760
ISSN (online)	1945-2403
ISSN	0146-4760
DOI	10.1093/jat/bkv140
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Zs.A 1333: Show issues

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Article: Exploring protein-protein interactions involving newly synthesized mitochondrial DNA-encoded proteins.

Horn, Darryl / Fontanesi, Flavia / Barrientos, Antoni

Methods in molecular biology (Clifton, N.J.)

2008 Volume 457, Page(s) 125–139

Abstract: Biogenesis of the mitochondrial respiratory chain enzymes involves the coordinated action of the mitochondrial and nuclear genomes. As a matter of fact, the structural sub-units forming these multimeric enzymes are encoded in both genomes. In addition, ... ...

Abstract	Biogenesis of the mitochondrial respiratory chain enzymes involves the coordinated action of the mitochondrial and nuclear genomes. As a matter of fact, the structural sub-units forming these multimeric enzymes are encoded in both genomes. In addition, the assistance of nuclear encoded factors, termed assembly factors, is necessary to allow for the expression of the mitochondrial DNA-encoded subunits and to facilitate their maturation, membrane insertion, and further assembly into the corresponding enzymatic complex. These processes involve transient interactions among the newly synthesized mitochondrial products and specific assembly factors. The identification and characterization of these interactions can be achieved by the method described here, consisting of pulling down tagged versions of the assembly factors immediately after radiolabeling the mitochondrial translation products in isolated mitochondria, and analyzing the radiolabeled pulled-down material.
MeSH term(s)	DNA, Mitochondrial/genetics ; Immunoprecipitation ; Mitochondrial Proteins/biosynthesis ; Protein Biosynthesis ; Protein Interaction Mapping/methods ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	DNA, Mitochondrial ; Mitochondrial Proteins ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2008-11-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1007/978-1-59745-261-8_9
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Article ; Online: Cmc1p is a conserved mitochondrial twin CX9C protein involved in cytochrome c oxidase biogenesis.

Horn, Darryl / Al-Ali, Hassan / Barrientos, Antoni

Molecular and cellular biology

2008 Volume 28, Issue 13, Page(s) 4354–4364

Abstract: Copper is an essential cofactor of two mitochondrial enzymes: cytochrome c oxidase (COX) and Cu-Zn superoxide dismutase (Sod1p). Copper incorporation into these enzymes is facilitated by metallochaperone proteins which probably use copper from a ... ...

Abstract	Copper is an essential cofactor of two mitochondrial enzymes: cytochrome c oxidase (COX) and Cu-Zn superoxide dismutase (Sod1p). Copper incorporation into these enzymes is facilitated by metallochaperone proteins which probably use copper from a mitochondrial matrix-localized pool. Here we describe a novel conserved mitochondrial metallochaperone-like protein, Cmc1p, whose function affects both COX and Sod1p. In Saccharomyces cerevisiae, Cmc1p localizes to the mitochondrial inner membrane facing the intermembrane space. Cmc1p is essential for full expression of COX and respiration, contains a twin CX9C domain conserved in other COX assembly copper chaperones, and has the ability to bind copper(I). Additionally, mutant cmc1 cells display increased mitochondrial Sod1p activity, while CMC1 overexpression results in decreased Sod1p activity. Our results suggest that Cmc1p could play a direct or indirect role in copper trafficking and distribution to COX and Sod1p.
MeSH term(s)	Amino Acid Sequence ; Carrier Proteins/chemistry ; Carrier Proteins/isolation & purification ; Carrier Proteins/metabolism ; Conserved Sequence ; Copper/pharmacology ; Electron Transport Complex IV/metabolism ; HeLa Cells ; Humans ; Metallochaperones ; Mitochondria/drug effects ; Mitochondria/enzymology ; Mitochondrial Membranes/drug effects ; Mitochondrial Membranes/enzymology ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/isolation & purification ; Mitochondrial Proteins/metabolism ; Molecular Sequence Data ; Molecular Weight ; Mutant Proteins/metabolism ; Mutation/genetics ; Protein Binding/drug effects ; Protein Structure, Tertiary ; Protein Transport/drug effects ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/isolation & purification ; Saccharomyces cerevisiae Proteins/metabolism ; Superoxide Dismutase/metabolism
Chemical Substances	CMC1 protein, S cerevisiae ; Carrier Proteins ; Metallochaperones ; Mitochondrial Proteins ; Mutant Proteins ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Copper (789U1901C5) ; Superoxide Dismutase (EC 1.15.1.1) ; Electron Transport Complex IV (EC 1.9.3.1)
Language	English
Publishing date	2008-04-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.01920-07
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Article ; Online: Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.

Neal, Sonya E / Dabir, Deepa V / Tienson, Heather L / Horn, Darryl M / Glaeser, Kathrin / Ogozalek Loo, Rachel R / Barrientos, Antoni / Koehler, Carla M

The Journal of biological chemistry

2015 Volume 290, Issue 34, Page(s) 20804–20814

Abstract: A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. ... ...

Abstract	A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation. In this study, we have addressed the oxidation of Tim13 in vitro and in organello. Reductants such as glutathione and ascorbate inhibited both the oxidation of the substrate Tim13 in vitro and the import of Tim13 and Cmc1 into isolated mitochondria. In addition, a ternary complex consisting of Erv1, Mia40, and substrate, linked by disulfide bonds, was not detected in vitro. Instead, Mia40 accepted six electrons from substrates, and this fully reduced Mia40 was sensitive to protease, indicative of conformational changes in the structure. Mia40 in mitochondria from the erv1-101 mutant was also trapped in a completely reduced state, demonstrating that Mia40 can accept up to six electrons as substrates are imported. Therefore, these studies support that Mia40 functions as an electron sink to facilitate the insertion of two disulfide bonds into substrates.
MeSH term(s)	Ascorbic Acid/pharmacology ; Disulfides/chemistry ; Disulfides/metabolism ; Electrons ; Gene Expression Regulation, Fungal ; Glutathione/pharmacology ; Metallochaperones/genetics ; Metallochaperones/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation ; Oxidation-Reduction ; Oxidoreductases Acting on Sulfur Group Donors/genetics ; Oxidoreductases Acting on Sulfur Group Donors/metabolism ; Plasmids/chemistry ; Plasmids/metabolism ; Protein Transport ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Reducing Agents/pharmacology ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
Chemical Substances	CMC1 protein, S cerevisiae ; Disulfides ; MIA40 protein, S cerevisiae ; Metallochaperones ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Recombinant Proteins ; Reducing Agents ; Saccharomyces cerevisiae Proteins ; TIM13 protein, S cerevisiae ; Oxidoreductases Acting on Sulfur Group Donors (EC 1.8.-) ; ERV1 protein, S cerevisiae (EC 1.8.3.2) ; Glutathione (GAN16C9B8O) ; Ascorbic Acid (PQ6CK8PD0R)
Language	English
Publishing date	2015-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.669440
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Article ; Online: Mss51 and Ssc1 facilitate translational regulation of cytochrome c oxidase biogenesis.

Fontanesi, Flavia / Soto, Iliana C / Horn, Darryl / Barrientos, Antoni

Molecular and cellular biology

2009 Volume 30, Issue 1, Page(s) 245–259

Abstract: The intricate biogenesis of multimeric organellar enzymes of dual genetic origin entails several levels of regulation. In Saccharomyces cerevisiae, mitochondrial cytochrome c oxidase (COX) assembly is regulated translationally. Synthesis of subunit 1 ( ... ...

Abstract	The intricate biogenesis of multimeric organellar enzymes of dual genetic origin entails several levels of regulation. In Saccharomyces cerevisiae, mitochondrial cytochrome c oxidase (COX) assembly is regulated translationally. Synthesis of subunit 1 (Cox1) is contingent on the availability of its assembly partners, thereby acting as a negative feedback loop that coordinates COX1 mRNA translation with Cox1 utilization during COX assembly. The COX1 mRNA-specific translational activator Mss51 plays a fundamental role in this process. Here, we report that Mss51 successively interacts with the COX1 mRNA translational apparatus, newly synthesized Cox1, and other COX assembly factors during Cox1 maturation/assembly. Notably, the mitochondrial Hsp70 chaperone Ssc1 is shown to be an Mss51 partner throughout its metabolic cycle. We conclude that Ssc1, by interacting with Mss51 and Mss51-containing complexes, plays a critical role in Cox1 biogenesis, COX assembly, and the translational regulation of these processes.
MeSH term(s)	Calcium-Transporting ATPases/physiology ; Electron Transport Complex IV/biosynthesis ; Electron Transport Complex IV/genetics ; Molecular Chaperones/physiology ; Molecular Weight ; Mutation ; Protein Biosynthesis ; Protein Interaction Mapping ; Protein Subunits/biosynthesis ; Protein Subunits/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; Transcription Factors/physiology
Chemical Substances	Molecular Chaperones ; Mss51 protein, S cerevisiae ; Protein Subunits ; SSC1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; Electron Transport Complex IV (EC 1.9.3.1) ; Calcium-Transporting ATPases (EC 7.2.2.10)
Language	English
Publishing date	2009-10-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00983-09
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Article: Synthesis of cytochrome c oxidase subunit 1 is translationally downregulated in the absence of functional F1F0-ATP synthase.

Soto, Ileana C / Fontanesi, Flavia / Valledor, Melvys / Horn, Darryl / Singh, Rajiv / Barrientos, Antoni

Biochimica et biophysica acta

2009 Volume 1793, Issue 11, Page(s) 1776–1786

Abstract: The mitochondrial F(1)F(0)-ATP synthase or ATPase is a key enzyme for aerobic energy production in eukaryotic cells. Mutations in ATPase structural and assembly genes are the primary cause of severe human encephalomyopathies, frequently associated with a ...

Abstract	The mitochondrial F(1)F(0)-ATP synthase or ATPase is a key enzyme for aerobic energy production in eukaryotic cells. Mutations in ATPase structural and assembly genes are the primary cause of severe human encephalomyopathies, frequently associated with a pleiotropic decrease in cytochrome c oxidase (COX) activity. We have studied the structural and functional constraints underlying the COX defect using Saccharomyces cerevisiae genetic and pharmacological models of ATPase deficiency. In both yeast Deltaatp10 and oligomycin-treated wild type cells, COX assembly is selectively impaired in the absence of functional ATPase. The COX biogenesis defect does not involve a primary alteration in the expression of the COX subunits as previously suggested but in their maturation and/or assembly. Expression of COX subunit 1, however, is translationally regulated as in most bona fide COX assembly mutants. Additionally, the COX defect in oligomycin-inhibited ATPase-deficient yeast cells, but not in atp10 cells could be partially prevented by partially dissipating the mitochondrial membrane potential using the uncoupler CCCP. Similar results were obtained with oligomycin-treated and ATP12-deficient human fibroblasts respectively. Our findings imply that fully assembled ATPase and its proton pumping function are both required for COX biogenesis in yeast and mammalian cells through a mechanism independent of Cox1p synthesis.
MeSH term(s)	Aerobiosis/genetics ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Electron Transport Complex IV ; Fibroblasts/enzymology ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Fungal ; H(+)-K(+)-Exchanging ATPase/genetics ; Humans ; Mitochondrial Encephalomyopathies/enzymology ; Mitochondrial Encephalomyopathies/genetics ; Models, Biological ; Mutation ; Oligomycins/pharmacology ; Proton-Translocating ATPases ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins ; Uncoupling Agents/pharmacology
Chemical Substances	Oligomycins ; Saccharomyces cerevisiae Proteins ; Uncoupling Agents ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2) ; Cox1 protein, S cerevisiae (EC 1.9.3.1) ; Electron Transport Complex IV (EC 1.9.3.1) ; H(+)-K(+)-Exchanging ATPase (EC 3.6.3.10) ; Proton-Translocating ATPases (EC 3.6.3.14)
Language	English
Publishing date	2009-09-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2009.09.002
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Article: Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process.

Fontanesi, Flavia / Soto, Ileana C / Horn, Darryl / Barrientos, Antoni

American journal of physiology. Cell physiology

2006 Volume 291, Issue 6, Page(s) C1129–47

Abstract: Cytochrome c-oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, plays a key role in the regulation of aerobic production of energy. Biogenesis of eukaryotic COX involves the coordinated action of two genomes. Three mitochondrial ... ...

Abstract	Cytochrome c-oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, plays a key role in the regulation of aerobic production of energy. Biogenesis of eukaryotic COX involves the coordinated action of two genomes. Three mitochondrial DNA-encoded subunits form the catalytic core of the enzyme, which contains metal prosthetic groups. Another 10 subunits encoded in the nuclear DNA act as a protective shield surrounding the core. COX biogenesis requires the assistance of >20 additional nuclear-encoded factors acting at all levels of the process. Expression of the mitochondrial-encoded subunits, expression and import of the nuclear-encoded subunits, insertion of the structural subunits into the mitochondrial inner membrane, addition of prosthetic groups, assembly of the holoenzyme, further maturation to form a dimer, and additional assembly into supercomplexes are all tightly regulated processes in a nuclear-mitochondrial-coordinated fashion. Such regulation ensures the building of a highly efficient machine able to catalyze the safe transfer of electrons from cytochrome c to molecular oxygen and ultimately facilitate the aerobic production of ATP. In this review, we will focus on describing and analyzing the present knowledge about the different regulatory checkpoints in COX assembly and the dynamic relationships between the different factors involved in the process. We have used information mostly obtained from the suitable yeast model, but also from bacterial and animal systems, by means of large-scale genetic, molecular biology, and physiological approaches and by integrating information concerning individual elements into a cellular system network.
MeSH term(s)	Animals ; Carbon/metabolism ; Electron Transport Complex IV/biosynthesis ; Electron Transport Complex IV/genetics ; Gene Expression Regulation ; Mitochondria/enzymology ; Mitochondria/genetics ; Oxidative Phosphorylation ; Oxygen/metabolism ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction/physiology ; Transcription, Genetic
Chemical Substances	Protein Subunits ; Saccharomyces cerevisiae Proteins ; Carbon (7440-44-0) ; Electron Transport Complex IV (EC 1.9.3.1) ; Oxygen (S88TT14065)
Language	English
Publishing date	2006-06-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00233.2006
Database	MEDical Literature Analysis and Retrieval System OnLINE

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