The Complexity of Mitochondrial Complex IV: An Update of Cytochrome c Oxidase Biogenesis in Plants
Mitochondrial respiration is an energy producing process that involves the coordinated action of several protein complexes embedded in the inner membrane to finally produce ATP. Complex IV or Cytochrome Oxidase (COX) is the last electron acceptor of the respiratory chain, involved in the reduction o...
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| Veröffentlicht in: | International journal of molecular sciences 2018-02, Vol.19 (3), p.662 |
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| description | Mitochondrial respiration is an energy producing process that involves the coordinated action of several protein complexes embedded in the inner membrane to finally produce ATP. Complex IV or Cytochrome
Oxidase (COX) is the last electron acceptor of the respiratory chain, involved in the reduction of O₂ to H₂O. COX is a multimeric complex formed by multiple structural subunits encoded in two different genomes, prosthetic groups (heme
and heme
₃), and metallic centers (Cu
and Cu
). Tens of accessory proteins are required for mitochondrial RNA processing, synthesis and delivery of prosthetic groups and metallic centers, and for the final assembly of subunits to build a functional complex. In this review, we perform a comparative analysis of COX composition and biogenesis factors in yeast, mammals and plants. We also describe possible external and internal factors controlling the expression of structural proteins and assembly factors at the transcriptional and post-translational levels, and the effect of deficiencies in different steps of COX biogenesis to infer the role of COX in different aspects of plant development. We conclude that COX assembly in plants has conserved and specific features, probably due to the incorporation of a different set of subunits during evolution. |
| doi_str_mv | 10.3390/ijms19030662 |
| format | Article |
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Oxidase (COX) is the last electron acceptor of the respiratory chain, involved in the reduction of O₂ to H₂O. COX is a multimeric complex formed by multiple structural subunits encoded in two different genomes, prosthetic groups (heme
and heme
₃), and metallic centers (Cu
and Cu
). Tens of accessory proteins are required for mitochondrial RNA processing, synthesis and delivery of prosthetic groups and metallic centers, and for the final assembly of subunits to build a functional complex. In this review, we perform a comparative analysis of COX composition and biogenesis factors in yeast, mammals and plants. We also describe possible external and internal factors controlling the expression of structural proteins and assembly factors at the transcriptional and post-translational levels, and the effect of deficiencies in different steps of COX biogenesis to infer the role of COX in different aspects of plant development. We conclude that COX assembly in plants has conserved and specific features, probably due to the incorporation of a different set of subunits during evolution.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms19030662</identifier><identifier>PMID: 29495437</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Animals ; Biosynthesis ; Catalytic Domain ; Comparative analysis ; Cytochrome ; Cytochrome-c oxidase ; Electron transport ; Electron Transport Complex IV - chemistry ; Electron Transport Complex IV - genetics ; Electron Transport Complex IV - metabolism ; Energy Metabolism ; Enzyme Activation ; Gene Expression Regulation, Plant ; Genomes ; Heme ; Humans ; Mammals - genetics ; Mammals - metabolism ; Mitochondria ; Mitochondria - genetics ; Mitochondria - metabolism ; Mitochondrial DNA ; Mutation ; Plant Development ; Plant Physiological Phenomena ; Plants (botany) ; Plants - genetics ; Plants - metabolism ; Post-translation ; Prostheses ; Prosthetic groups ; Protein Subunits ; Proteins ; Review ; RNA processing ; Structural proteins ; Transcription factors ; Yeast ; Yeasts - genetics ; Yeasts - metabolism</subject><ispartof>International journal of molecular sciences, 2018-02, Vol.19 (3), p.662</ispartof><rights>2018. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2018 by the authors. 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-32da8bc5d6100ead6a2f219f775c671b513d9280e36a0dff8d64a2c9e88c10c13</citedby><cites>FETCH-LOGICAL-c478t-32da8bc5d6100ead6a2f219f775c671b513d9280e36a0dff8d64a2c9e88c10c13</cites><orcidid>0000-0001-7470-9635</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/PMC5877523/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5877523/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29495437$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mansilla, Natanael</creatorcontrib><creatorcontrib>Racca, Sofia</creatorcontrib><creatorcontrib>Gras, Diana E</creatorcontrib><creatorcontrib>Gonzalez, Daniel H</creatorcontrib><creatorcontrib>Welchen, Elina</creatorcontrib><title>The Complexity of Mitochondrial Complex IV: An Update of Cytochrome c Oxidase Biogenesis in Plants</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Mitochondrial respiration is an energy producing process that involves the coordinated action of several protein complexes embedded in the inner membrane to finally produce ATP. Complex IV or Cytochrome
Oxidase (COX) is the last electron acceptor of the respiratory chain, involved in the reduction of O₂ to H₂O. COX is a multimeric complex formed by multiple structural subunits encoded in two different genomes, prosthetic groups (heme
and heme
₃), and metallic centers (Cu
and Cu
). Tens of accessory proteins are required for mitochondrial RNA processing, synthesis and delivery of prosthetic groups and metallic centers, and for the final assembly of subunits to build a functional complex. In this review, we perform a comparative analysis of COX composition and biogenesis factors in yeast, mammals and plants. We also describe possible external and internal factors controlling the expression of structural proteins and assembly factors at the transcriptional and post-translational levels, and the effect of deficiencies in different steps of COX biogenesis to infer the role of COX in different aspects of plant development. We conclude that COX assembly in plants has conserved and specific features, probably due to the incorporation of a different set of subunits during evolution.</description><subject>Animals</subject><subject>Biosynthesis</subject><subject>Catalytic Domain</subject><subject>Comparative analysis</subject><subject>Cytochrome</subject><subject>Cytochrome-c oxidase</subject><subject>Electron transport</subject><subject>Electron Transport Complex IV - chemistry</subject><subject>Electron Transport Complex IV - genetics</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Energy Metabolism</subject><subject>Enzyme Activation</subject><subject>Gene Expression Regulation, Plant</subject><subject>Genomes</subject><subject>Heme</subject><subject>Humans</subject><subject>Mammals - genetics</subject><subject>Mammals - metabolism</subject><subject>Mitochondria</subject><subject>Mitochondria - genetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial DNA</subject><subject>Mutation</subject><subject>Plant Development</subject><subject>Plant Physiological Phenomena</subject><subject>Plants (botany)</subject><subject>Plants - genetics</subject><subject>Plants - metabolism</subject><subject>Post-translation</subject><subject>Prostheses</subject><subject>Prosthetic groups</subject><subject>Protein Subunits</subject><subject>Proteins</subject><subject>Review</subject><subject>RNA processing</subject><subject>Structural proteins</subject><subject>Transcription factors</subject><subject>Yeast</subject><subject>Yeasts - genetics</subject><subject>Yeasts - metabolism</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc1LAzEQxYMoft88S8CLB6uTZDe760HQ4hcoemi9hjSZbVN2NzXZiv3v3aKW6mkG3o8383iEHDE4F6KACzetIytAgJR8g-yyhPMegMw21_YdshfjFIALnhbbZIcXSZEmItslo8EEad_Xswo_XbugvqTPrvVm4hsbnK5-Nfr4dkmvGzqcWd3iEusvlljwNVJDXz6d1RHpjfNjbDC6SF1DXyvdtPGAbJW6inj4M_fJ8O520H_oPb3cP_avn3omyfK2J7jV-cikVjIA1FZqXnJWlFmWGpmxUcqELXgOKKQGW5a5lYnmpsA8NwwME_vk6tt3Nh_VaA02bdCVmgVX67BQXjv1V2ncRI39h0rz7gYXncHpj0Hw73OMrapdNFh1KdDPo-LAQGSSZUmHnvxDp34emi6e4gzypHs2WRqefVMm-BgDlqtnGKhleWq9vA4_Xg-wgn_bEl_UdJWs</recordid><startdate>20180227</startdate><enddate>20180227</enddate><creator>Mansilla, Natanael</creator><creator>Racca, Sofia</creator><creator>Gras, Diana E</creator><creator>Gonzalez, Daniel H</creator><creator>Welchen, Elina</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-7470-9635</orcidid></search><sort><creationdate>20180227</creationdate><title>The Complexity of Mitochondrial Complex IV: An Update of Cytochrome c Oxidase Biogenesis in Plants</title><author>Mansilla, Natanael ; Racca, Sofia ; Gras, Diana E ; Gonzalez, Daniel H ; Welchen, Elina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-32da8bc5d6100ead6a2f219f775c671b513d9280e36a0dff8d64a2c9e88c10c13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animals</topic><topic>Biosynthesis</topic><topic>Catalytic Domain</topic><topic>Comparative analysis</topic><topic>Cytochrome</topic><topic>Cytochrome-c oxidase</topic><topic>Electron transport</topic><topic>Electron Transport Complex IV - chemistry</topic><topic>Electron Transport Complex IV - genetics</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Energy Metabolism</topic><topic>Enzyme Activation</topic><topic>Gene Expression Regulation, Plant</topic><topic>Genomes</topic><topic>Heme</topic><topic>Humans</topic><topic>Mammals - genetics</topic><topic>Mammals - metabolism</topic><topic>Mitochondria</topic><topic>Mitochondria - genetics</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial DNA</topic><topic>Mutation</topic><topic>Plant Development</topic><topic>Plant Physiological Phenomena</topic><topic>Plants (botany)</topic><topic>Plants - genetics</topic><topic>Plants - metabolism</topic><topic>Post-translation</topic><topic>Prostheses</topic><topic>Prosthetic groups</topic><topic>Protein Subunits</topic><topic>Proteins</topic><topic>Review</topic><topic>RNA processing</topic><topic>Structural proteins</topic><topic>Transcription factors</topic><topic>Yeast</topic><topic>Yeasts - genetics</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mansilla, Natanael</creatorcontrib><creatorcontrib>Racca, Sofia</creatorcontrib><creatorcontrib>Gras, Diana E</creatorcontrib><creatorcontrib>Gonzalez, Daniel H</creatorcontrib><creatorcontrib>Welchen, Elina</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Proquest Health & Medical Complete</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mansilla, Natanael</au><au>Racca, Sofia</au><au>Gras, Diana E</au><au>Gonzalez, Daniel H</au><au>Welchen, Elina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Complexity of Mitochondrial Complex IV: An Update of Cytochrome c Oxidase Biogenesis in Plants</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2018-02-27</date><risdate>2018</risdate><volume>19</volume><issue>3</issue><spage>662</spage><pages>662-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Mitochondrial respiration is an energy producing process that involves the coordinated action of several protein complexes embedded in the inner membrane to finally produce ATP. Complex IV or Cytochrome
Oxidase (COX) is the last electron acceptor of the respiratory chain, involved in the reduction of O₂ to H₂O. COX is a multimeric complex formed by multiple structural subunits encoded in two different genomes, prosthetic groups (heme
and heme
₃), and metallic centers (Cu
and Cu
). Tens of accessory proteins are required for mitochondrial RNA processing, synthesis and delivery of prosthetic groups and metallic centers, and for the final assembly of subunits to build a functional complex. In this review, we perform a comparative analysis of COX composition and biogenesis factors in yeast, mammals and plants. We also describe possible external and internal factors controlling the expression of structural proteins and assembly factors at the transcriptional and post-translational levels, and the effect of deficiencies in different steps of COX biogenesis to infer the role of COX in different aspects of plant development. We conclude that COX assembly in plants has conserved and specific features, probably due to the incorporation of a different set of subunits during evolution.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>29495437</pmid><doi>10.3390/ijms19030662</doi><orcidid>https://orcid.org/0000-0001-7470-9635</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Biosynthesis Catalytic Domain Comparative analysis Cytochrome Cytochrome-c oxidase Electron transport Electron Transport Complex IV - chemistry Electron Transport Complex IV - genetics Electron Transport Complex IV - metabolism Energy Metabolism Enzyme Activation Gene Expression Regulation, Plant Genomes Heme Humans Mammals - genetics Mammals - metabolism Mitochondria Mitochondria - genetics Mitochondria - metabolism Mitochondrial DNA Mutation Plant Development Plant Physiological Phenomena Plants (botany) Plants - genetics Plants - metabolism Post-translation Prostheses Prosthetic groups Protein Subunits Proteins Review RNA processing Structural proteins Transcription factors Yeast Yeasts - genetics Yeasts - metabolism |
| title | The Complexity of Mitochondrial Complex IV: An Update of Cytochrome c Oxidase Biogenesis in Plants |
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