ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis
Summary Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for c...
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| Veröffentlicht in: | Molecular microbiology 2006-07, Vol.61 (1), p.219-231 |
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| creator | Feissner, Robert E. Richard‐Fogal, Cynthia L. Frawley, Elaine R. Kranz, Robert G. |
| description | Summary
Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for cytochrome c biogenesis. Here, we show the mechanism by which the system I pathway can utilize haem at low levels. The mechanism involves an ATP‐binding cassette (ABC) transporter that is required for release of the periplasmic haem chaperone CcmE to the last step of cytochrome c assembly. This ABC transporter is composed of the ABC subunit CcmA, and two membrane proteins, CcmB and CcmC. In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead‐end complex, indicating high affinity binding of haem to CcmC. Expression of CcmA and CcmB facilitates formation of the CcmA2B1C1 complex and ATP‐dependent release of holoCcmE. We propose that the CcmA2B1C1 complex represents a new subgroup within the ABC transporter superfamily that functions to release a chaperone. |
| doi_str_mv | 10.1111/j.1365-2958.2006.05221.x |
| format | Article |
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Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for cytochrome c biogenesis. Here, we show the mechanism by which the system I pathway can utilize haem at low levels. The mechanism involves an ATP‐binding cassette (ABC) transporter that is required for release of the periplasmic haem chaperone CcmE to the last step of cytochrome c assembly. This ABC transporter is composed of the ABC subunit CcmA, and two membrane proteins, CcmB and CcmC. In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead‐end complex, indicating high affinity binding of haem to CcmC. Expression of CcmA and CcmB facilitates formation of the CcmA2B1C1 complex and ATP‐dependent release of holoCcmE. We propose that the CcmA2B1C1 complex represents a new subgroup within the ABC transporter superfamily that functions to release a chaperone.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2006.05221.x</identifier><identifier>PMID: 16824107</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Apoproteins - metabolism ; ATP-Binding Cassette Transporters - genetics ; ATP-Binding Cassette Transporters - metabolism ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biological and medical sciences ; Biological Transport ; Cytochrome c Group - biosynthesis ; E coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Genes ; Heme - metabolism ; Hemeproteins - biosynthesis ; Hemeproteins - genetics ; Hemeproteins - metabolism ; Immunology ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microbiology ; Models, Biological ; Molecular Chaperones - metabolism ; Plasmids - genetics ; Recombinant Fusion Proteins - metabolism</subject><ispartof>Molecular microbiology, 2006-07, Vol.61 (1), p.219-231</ispartof><rights>2006 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Jul 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4551-42b64909110886772f0c92087a7d91ef691dba1b9063e3e0f05fce1e9d248eed3</citedby><cites>FETCH-LOGICAL-c4551-42b64909110886772f0c92087a7d91ef691dba1b9063e3e0f05fce1e9d248eed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2958.2006.05221.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2006.05221.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27903,27904,45553,45554,46387,46811</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17877772$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16824107$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Feissner, Robert E.</creatorcontrib><creatorcontrib>Richard‐Fogal, Cynthia L.</creatorcontrib><creatorcontrib>Frawley, Elaine R.</creatorcontrib><creatorcontrib>Kranz, Robert G.</creatorcontrib><title>ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for cytochrome c biogenesis. Here, we show the mechanism by which the system I pathway can utilize haem at low levels. The mechanism involves an ATP‐binding cassette (ABC) transporter that is required for release of the periplasmic haem chaperone CcmE to the last step of cytochrome c assembly. This ABC transporter is composed of the ABC subunit CcmA, and two membrane proteins, CcmB and CcmC. In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead‐end complex, indicating high affinity binding of haem to CcmC. Expression of CcmA and CcmB facilitates formation of the CcmA2B1C1 complex and ATP‐dependent release of holoCcmE. We propose that the CcmA2B1C1 complex represents a new subgroup within the ABC transporter superfamily that functions to release a chaperone.</description><subject>Apoproteins - metabolism</subject><subject>ATP-Binding Cassette Transporters - genetics</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Cytochrome c Group - biosynthesis</subject><subject>E coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Heme - metabolism</subject><subject>Hemeproteins - biosynthesis</subject><subject>Hemeproteins - genetics</subject><subject>Hemeproteins - metabolism</subject><subject>Immunology</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Microbiology</subject><subject>Models, Biological</subject><subject>Molecular Chaperones - metabolism</subject><subject>Plasmids - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAQgC0EokvhFZCFBLcEjx079oFDWfFTqRUXKnGzHGfCZpXEi51VuzcegWfkSXDYFZW4wFxsab4ZzcxHCAVWQo7X2xKEkgU3UpecMVUyyTmUdw_I6k_iIVkxI1khNP9yRp6ktGUMBFPiMTkDpXkFrF6Rm4u3azpHN6VdiDPGn99_jNj2bsaWRhzQJaSho45uHI7Ub9wOY5iQumEIt4n6wxz8JoYRqadNH77ihKlPT8mjzg0Jn53ec3Lz_t3n9cfi6tOHy_XFVeErKaGoeKMqwwwA01rVNe-YN5zp2tWtAeyUgbZx0Jg8NQpkHZOdR0DT8kojtuKcvDr23cXwbY9ptmOfPA6DmzDsk1VagZLS_BMEI0CB1Bl88Re4Dfs45SUyo2TFhWQZ0kfIx5BSxM7uYj-6eLDA7CLIbu3iwS4e7CLI_hZk73Lp81P_fZMPfV94MpKBlyfAJe-GLqvxfbrnal3n4Jl7c-Ru-wEP_z2Avb6-XH7iF7Rdq1s</recordid><startdate>200607</startdate><enddate>200607</enddate><creator>Feissner, Robert E.</creator><creator>Richard‐Fogal, Cynthia L.</creator><creator>Frawley, Elaine R.</creator><creator>Kranz, Robert G.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell Science</general><scope>IQODW</scope><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200607</creationdate><title>ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis</title><author>Feissner, Robert E. ; Richard‐Fogal, Cynthia L. ; Frawley, Elaine R. ; Kranz, Robert G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4551-42b64909110886772f0c92087a7d91ef691dba1b9063e3e0f05fce1e9d248eed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Apoproteins - metabolism</topic><topic>ATP-Binding Cassette Transporters - genetics</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Cytochrome c Group - biosynthesis</topic><topic>E coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Heme - metabolism</topic><topic>Hemeproteins - biosynthesis</topic><topic>Hemeproteins - genetics</topic><topic>Hemeproteins - metabolism</topic><topic>Immunology</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Microbiology</topic><topic>Models, Biological</topic><topic>Molecular Chaperones - metabolism</topic><topic>Plasmids - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feissner, Robert E.</creatorcontrib><creatorcontrib>Richard‐Fogal, Cynthia L.</creatorcontrib><creatorcontrib>Frawley, Elaine R.</creatorcontrib><creatorcontrib>Kranz, Robert G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feissner, Robert E.</au><au>Richard‐Fogal, Cynthia L.</au><au>Frawley, Elaine R.</au><au>Kranz, Robert G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2006-07</date><risdate>2006</risdate><volume>61</volume><issue>1</issue><spage>219</spage><epage>231</epage><pages>219-231</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for cytochrome c biogenesis. Here, we show the mechanism by which the system I pathway can utilize haem at low levels. The mechanism involves an ATP‐binding cassette (ABC) transporter that is required for release of the periplasmic haem chaperone CcmE to the last step of cytochrome c assembly. This ABC transporter is composed of the ABC subunit CcmA, and two membrane proteins, CcmB and CcmC. In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead‐end complex, indicating high affinity binding of haem to CcmC. Expression of CcmA and CcmB facilitates formation of the CcmA2B1C1 complex and ATP‐dependent release of holoCcmE. We propose that the CcmA2B1C1 complex represents a new subgroup within the ABC transporter superfamily that functions to release a chaperone.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>16824107</pmid><doi>10.1111/j.1365-2958.2006.05221.x</doi><tpages>13</tpages></addata></record> |
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| ispartof | Molecular microbiology, 2006-07, Vol.61 (1), p.219-231 |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Apoproteins - metabolism ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological and medical sciences Biological Transport Cytochrome c Group - biosynthesis E coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Genes Heme - metabolism Hemeproteins - biosynthesis Hemeproteins - genetics Hemeproteins - metabolism Immunology Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Models, Biological Molecular Chaperones - metabolism Plasmids - genetics Recombinant Fusion Proteins - metabolism |
| title | ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis |
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