CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B
The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits assoc...
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| creator | Brischigliaro, Michele Cabrera‐Orefice, Alfredo Sturlese, Mattia Elurbe, Dei M Frigo, Elena Fernandez‐Vizarra, Erika Moro, Stefano Huynen, Martijn A Arnold, Susanne Viscomi, Carlo Zeviani, Massimo |
| description | The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits associated with redox prosthetic groups. These enzymes, which are the “core” redox centers of respiration, acquired additional subunits, and increased their complexity throughout evolution. Cytochrome
c
oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX composition in the invertebrate model
Drosophila melanogaster
. We identified and characterized a novel subunit which is widely different in amino acid sequence, but similar in secondary and tertiary structures to COX7B, and provided evidence that this object is in fact replacing the latter subunit in virtually all protostome invertebrates. These results demonstrate that although individual structures may differ the composition of COX is functionally conserved between vertebrate and invertebrate species.
Synopsis
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.
CG7630 is a structural component of COX in
D. melanogaster
.
Despite poor sequence similarity, CG7630 functionally corresponds to COX7B.
Invertebrate and mammalian COX enzymes have the same number of subunits.
The existence of CG7630 demonstrates divergent evolution of COX subunits in vertebrates and invertebrates.
Graphical Abstract
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
. |
| doi_str_mv | 10.15252/embr.202254825 |
| format | Article |
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c
oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX composition in the invertebrate model
Drosophila melanogaster
. We identified and characterized a novel subunit which is widely different in amino acid sequence, but similar in secondary and tertiary structures to COX7B, and provided evidence that this object is in fact replacing the latter subunit in virtually all protostome invertebrates. These results demonstrate that although individual structures may differ the composition of COX is functionally conserved between vertebrate and invertebrate species.
Synopsis
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.
CG7630 is a structural component of COX in
D. melanogaster
.
Despite poor sequence similarity, CG7630 functionally corresponds to COX7B.
Invertebrate and mammalian COX enzymes have the same number of subunits.
The existence of CG7630 demonstrates divergent evolution of COX subunits in vertebrates and invertebrates.
Graphical Abstract
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.202254825</identifier><identifier>PMID: 35699132</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino acid sequence ; Amino acids ; Composition ; COX7B ; Cytochrome ; Cytochrome-c oxidase ; Cytochromes ; D. melanogaster ; Divergence ; Drosophila melanogaster ; Electron transport ; EMBO21 ; Enzymes ; Evolution ; Fruit flies ; Homology ; Insects ; Invertebrates ; Mammals ; Mitochondria ; Oxidase ; Polypeptides ; Prostheses ; Prosthetic groups ; Proteomics ; respiratory chain ; Vertebrates</subject><ispartof>EMBO reports, 2022-08, Vol.23 (8), p.e54825-n/a</ispartof><rights>The Author(s) 2022</rights><rights>2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license</rights><rights>2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license.</rights><rights>2022. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5135-1fba549faec4d3fef5b62dc5f35ed27185f17bc50536a8ed9cc1bb320fa29d183</citedby><cites>FETCH-LOGICAL-c5135-1fba549faec4d3fef5b62dc5f35ed27185f17bc50536a8ed9cc1bb320fa29d183</cites><orcidid>0000-0002-2469-142X ; 0000-0003-1520-1342 ; 0000-0001-6050-0566 ; 0000-0001-6189-5491 ; 0000-0003-2667-5156 ; 0000-0002-2042-3794 ; 0000-0002-9067-5508</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9346487/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9346487/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,1418,1434,27929,27930,41125,42194,45579,45580,46414,46838,51581,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35699132$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brischigliaro, Michele</creatorcontrib><creatorcontrib>Cabrera‐Orefice, Alfredo</creatorcontrib><creatorcontrib>Sturlese, Mattia</creatorcontrib><creatorcontrib>Elurbe, Dei M</creatorcontrib><creatorcontrib>Frigo, Elena</creatorcontrib><creatorcontrib>Fernandez‐Vizarra, Erika</creatorcontrib><creatorcontrib>Moro, Stefano</creatorcontrib><creatorcontrib>Huynen, Martijn A</creatorcontrib><creatorcontrib>Arnold, Susanne</creatorcontrib><creatorcontrib>Viscomi, Carlo</creatorcontrib><creatorcontrib>Zeviani, Massimo</creatorcontrib><title>CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits associated with redox prosthetic groups. These enzymes, which are the “core” redox centers of respiration, acquired additional subunits, and increased their complexity throughout evolution. Cytochrome
c
oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX composition in the invertebrate model
Drosophila melanogaster
. We identified and characterized a novel subunit which is widely different in amino acid sequence, but similar in secondary and tertiary structures to COX7B, and provided evidence that this object is in fact replacing the latter subunit in virtually all protostome invertebrates. These results demonstrate that although individual structures may differ the composition of COX is functionally conserved between vertebrate and invertebrate species.
Synopsis
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.
CG7630 is a structural component of COX in
D. melanogaster
.
Despite poor sequence similarity, CG7630 functionally corresponds to COX7B.
Invertebrate and mammalian COX enzymes have the same number of subunits.
The existence of CG7630 demonstrates divergent evolution of COX subunits in vertebrates and invertebrates.
Graphical Abstract
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.</description><subject>Amino acid sequence</subject><subject>Amino acids</subject><subject>Composition</subject><subject>COX7B</subject><subject>Cytochrome</subject><subject>Cytochrome-c oxidase</subject><subject>Cytochromes</subject><subject>D. melanogaster</subject><subject>Divergence</subject><subject>Drosophila melanogaster</subject><subject>Electron transport</subject><subject>EMBO21</subject><subject>Enzymes</subject><subject>Evolution</subject><subject>Fruit flies</subject><subject>Homology</subject><subject>Insects</subject><subject>Invertebrates</subject><subject>Mammals</subject><subject>Mitochondria</subject><subject>Oxidase</subject><subject>Polypeptides</subject><subject>Prostheses</subject><subject>Prosthetic groups</subject><subject>Proteomics</subject><subject>respiratory chain</subject><subject>Vertebrates</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNqFkd1rFDEUxUNR-qXPvknAF1-2zcdkMvFBsNtahUqhKPYtZDI3OykzkzWZsd3_3rS7XasgPuVCfvdwzj0IvaLkiAom2DH0dTxihDFRVEzsoH1alGrGqayebWbG6PUeOkjphhAilKx20R4XpVKUs330fX4uS06wT3hsAZ_GkMKy9Z3BPXRmCAuTRoi4DX3owgIH94DZ1RhsG0OfRxzufGMS4DTV0-BHPL-8licv0HNnugQvN-8h-vbx7Ov80-zi8vzz_MPFzArKxYy62ohCOQO2aLgDJ-qSNVY4LqBhklbCUVlbQQQvTQWNspbWNWfEGaYaWvFD9H6tu5zqHhoLwxhNp5fR9yaudDBe__kz-FYvwk-teFEWlcwCbzcCMfyYII2698lCl8NDmJJmpSyFyNctMvrmL_QmTHHI8TKlZCY5u3d0vKZsvmWK4LZmKNEPpen70vS2tLzx-mmGLf_YUgberYFb38Hqf3r67MvJ1VN1sl5OeW9YQPzt-l-GfgHXSrRt</recordid><startdate>20220803</startdate><enddate>20220803</enddate><creator>Brischigliaro, Michele</creator><creator>Cabrera‐Orefice, Alfredo</creator><creator>Sturlese, Mattia</creator><creator>Elurbe, Dei M</creator><creator>Frigo, Elena</creator><creator>Fernandez‐Vizarra, Erika</creator><creator>Moro, Stefano</creator><creator>Huynen, Martijn A</creator><creator>Arnold, Susanne</creator><creator>Viscomi, Carlo</creator><creator>Zeviani, Massimo</creator><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</general><scope>C6C</scope><scope>24P</scope><scope>WIN</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2469-142X</orcidid><orcidid>https://orcid.org/0000-0003-1520-1342</orcidid><orcidid>https://orcid.org/0000-0001-6050-0566</orcidid><orcidid>https://orcid.org/0000-0001-6189-5491</orcidid><orcidid>https://orcid.org/0000-0003-2667-5156</orcidid><orcidid>https://orcid.org/0000-0002-2042-3794</orcidid><orcidid>https://orcid.org/0000-0002-9067-5508</orcidid></search><sort><creationdate>20220803</creationdate><title>CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B</title><author>Brischigliaro, Michele ; Cabrera‐Orefice, Alfredo ; Sturlese, Mattia ; Elurbe, Dei M ; Frigo, Elena ; Fernandez‐Vizarra, Erika ; Moro, Stefano ; Huynen, Martijn A ; Arnold, Susanne ; Viscomi, Carlo ; Zeviani, Massimo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5135-1fba549faec4d3fef5b62dc5f35ed27185f17bc50536a8ed9cc1bb320fa29d183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Amino acid sequence</topic><topic>Amino acids</topic><topic>Composition</topic><topic>COX7B</topic><topic>Cytochrome</topic><topic>Cytochrome-c oxidase</topic><topic>Cytochromes</topic><topic>D. melanogaster</topic><topic>Divergence</topic><topic>Drosophila melanogaster</topic><topic>Electron transport</topic><topic>EMBO21</topic><topic>Enzymes</topic><topic>Evolution</topic><topic>Fruit flies</topic><topic>Homology</topic><topic>Insects</topic><topic>Invertebrates</topic><topic>Mammals</topic><topic>Mitochondria</topic><topic>Oxidase</topic><topic>Polypeptides</topic><topic>Prostheses</topic><topic>Prosthetic groups</topic><topic>Proteomics</topic><topic>respiratory chain</topic><topic>Vertebrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brischigliaro, Michele</creatorcontrib><creatorcontrib>Cabrera‐Orefice, Alfredo</creatorcontrib><creatorcontrib>Sturlese, Mattia</creatorcontrib><creatorcontrib>Elurbe, Dei M</creatorcontrib><creatorcontrib>Frigo, Elena</creatorcontrib><creatorcontrib>Fernandez‐Vizarra, Erika</creatorcontrib><creatorcontrib>Moro, Stefano</creatorcontrib><creatorcontrib>Huynen, Martijn A</creatorcontrib><creatorcontrib>Arnold, Susanne</creatorcontrib><creatorcontrib>Viscomi, Carlo</creatorcontrib><creatorcontrib>Zeviani, Massimo</creatorcontrib><collection>Springer Nature OA/Free Journals</collection><collection>Wiley Online Library (Open Access Collection)</collection><collection>Wiley Online Library (Open Access Collection)</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brischigliaro, Michele</au><au>Cabrera‐Orefice, Alfredo</au><au>Sturlese, Mattia</au><au>Elurbe, Dei M</au><au>Frigo, Elena</au><au>Fernandez‐Vizarra, Erika</au><au>Moro, Stefano</au><au>Huynen, Martijn A</au><au>Arnold, Susanne</au><au>Viscomi, Carlo</au><au>Zeviani, Massimo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2022-08-03</date><risdate>2022</risdate><volume>23</volume><issue>8</issue><spage>e54825</spage><epage>n/a</epage><pages>e54825-n/a</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><abstract>The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits associated with redox prosthetic groups. These enzymes, which are the “core” redox centers of respiration, acquired additional subunits, and increased their complexity throughout evolution. Cytochrome
c
oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX composition in the invertebrate model
Drosophila melanogaster
. We identified and characterized a novel subunit which is widely different in amino acid sequence, but similar in secondary and tertiary structures to COX7B, and provided evidence that this object is in fact replacing the latter subunit in virtually all protostome invertebrates. These results demonstrate that although individual structures may differ the composition of COX is functionally conserved between vertebrate and invertebrate species.
Synopsis
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.
CG7630 is a structural component of COX in
D. melanogaster
.
Despite poor sequence similarity, CG7630 functionally corresponds to COX7B.
Invertebrate and mammalian COX enzymes have the same number of subunits.
The existence of CG7630 demonstrates divergent evolution of COX subunits in vertebrates and invertebrates.
Graphical Abstract
The mitochondrial cytochrome
c
oxidase subunit COX7B was thought to be mammalian specific. This study reveals that the evolutionarily divergent protein CG7630 is the functional ortholog of COX7B in
Drosophila melanogaster
.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>35699132</pmid><doi>10.15252/embr.202254825</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0002-2469-142X</orcidid><orcidid>https://orcid.org/0000-0003-1520-1342</orcidid><orcidid>https://orcid.org/0000-0001-6050-0566</orcidid><orcidid>https://orcid.org/0000-0001-6189-5491</orcidid><orcidid>https://orcid.org/0000-0003-2667-5156</orcidid><orcidid>https://orcid.org/0000-0002-2042-3794</orcidid><orcidid>https://orcid.org/0000-0002-9067-5508</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | EMBO reports, 2022-08, Vol.23 (8), p.e54825-n/a |
| issn | 1469-221X 1469-3178 |
| language | eng |
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| source | Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); PubMed Central; Springer Nature OA/Free Journals |
| subjects | Amino acid sequence Amino acids Composition COX7B Cytochrome Cytochrome-c oxidase Cytochromes D. melanogaster Divergence Drosophila melanogaster Electron transport EMBO21 Enzymes Evolution Fruit flies Homology Insects Invertebrates Mammals Mitochondria Oxidase Polypeptides Prostheses Prosthetic groups Proteomics respiratory chain Vertebrates |
| title | CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B |
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