Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)
Copper chaperone for superoxide dismutase 1 (SOD1), CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), a...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-08, Vol.109 (34), p.13555-13560 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 13560 |
|---|---|
| container_issue | 34 |
| container_start_page | 13555 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 109 |
| creator | Banci, Lucia Bertini, Ivano Cantini, Francesca Kozyreva, Tatiana Massagni, Chiara Palumaa, Peep Rubino, Jeffrey T Zovo, Kairit |
| description | Copper chaperone for superoxide dismutase 1 (SOD1), CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising one or two of the protein’s three domains. The synergy between electrospray ionization mass spectrometry (ESI-MS) and NMR is fully exploited. This is an in vitro study of this process at the molecular level. Domain 1 of hCCS is necessary to load hSOD1 with Cu(I), requiring the heterodimeric complex formation with hSOD1 fostered by the interaction with domain 2. Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57–Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer. |
| doi_str_mv | 10.1073/pnas.1207493109 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_1034801828</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>41700970</jstor_id><sourcerecordid>41700970</sourcerecordid><originalsourceid>FETCH-LOGICAL-c492t-751dede0896cbb613292780bfa889c33b331b3f81d4c283a5910be8d5d24a7cc3</originalsourceid><addsrcrecordid>eNpdks2PEyEYh4nRuLV69qSSeNk9dPd9gSlwMTH1Y0022UPdM2EYpjNNZ6gw48d_L7OtXfUCCe_DAy8_CHmJcIkg-dW-t-kSGUihOYJ-RGZ5xMVSaHhMZgBMLpRg4ow8S2kLALpQ8JScMaaWWvJiRsL12NmepnHvY_jZVp5WberGwSZPkZ4369sPeEE7O4zRDm3o6dDEMG4a2vaDj9bdr_1oh4Y29yIX9tlEXWMnYe9pHSKdJNm1Wq0vnpMntd0l_-I4z8ndp49fV9eLm9vPX1bvbxZOaDYsZIGVrzwovXRluUTONJMKytoqpR3nJedY8lphJRxT3BYaofSqKiomrHSOz8m7g3c_lp2vnO-HaHdmH9vOxl8m2Nb8W-nbxmzCd8MFk5DfZk7Oj4IYvo0-DaZrk_O7ne19GJNB4EIBqnz6nLz9D92GMfa5vXtKolAaM3V1oFwMKUVfny6DYKYwzRSmeQgz73j9dw8n_k96GaBHYNr5oNO5C4O8KCbk1QHZpiHEEyNQ5s8gIdffHOq1DcZuYpvM3ZoBLgGQaVEo_htB9bgH</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1034714891</pqid></control><display><type>article</type><title>Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Banci, Lucia ; Bertini, Ivano ; Cantini, Francesca ; Kozyreva, Tatiana ; Massagni, Chiara ; Palumaa, Peep ; Rubino, Jeffrey T ; Zovo, Kairit</creator><creatorcontrib>Banci, Lucia ; Bertini, Ivano ; Cantini, Francesca ; Kozyreva, Tatiana ; Massagni, Chiara ; Palumaa, Peep ; Rubino, Jeffrey T ; Zovo, Kairit</creatorcontrib><description>Copper chaperone for superoxide dismutase 1 (SOD1), CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising one or two of the protein’s three domains. The synergy between electrospray ionization mass spectrometry (ESI-MS) and NMR is fully exploited. This is an in vitro study of this process at the molecular level. Domain 1 of hCCS is necessary to load hSOD1 with Cu(I), requiring the heterodimeric complex formation with hSOD1 fostered by the interaction with domain 2. Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57–Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1207493109</identifier><identifier>PMID: 22869735</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Binding Sites ; Biochemistry ; Biological Sciences ; Catalysis ; Copper ; Copper - chemistry ; Cysteine - chemistry ; disulfide bonds ; Disulfides ; Disulfides - chemistry ; electrospray ionization mass spectrometry ; Humans ; in vitro studies ; Kinetics ; Lyases - chemistry ; Lyases - physiology ; Magnetic Resonance Spectroscopy - methods ; Mass spectrometry ; Molecular Chaperones - metabolism ; Monomers ; mutants ; Mutation ; NMR ; Nuclear magnetic resonance ; nuclear magnetic resonance spectroscopy ; Oxidation ; Oxidation-Reduction ; Oxygen ; Physiology ; Protein Binding ; Proteins ; Spectrometry, Mass, Electrospray Ionization - methods ; superoxide dismutase ; Superoxide Dismutase - genetics ; Superoxide Dismutase - physiology ; Superoxide Dismutase-1 ; Superoxides ; Time Factors ; Yeasts ; Zinc</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-08, Vol.109 (34), p.13555-13560</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Aug 21, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-751dede0896cbb613292780bfa889c33b331b3f81d4c283a5910be8d5d24a7cc3</citedby><cites>FETCH-LOGICAL-c492t-751dede0896cbb613292780bfa889c33b331b3f81d4c283a5910be8d5d24a7cc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/34.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41700970$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41700970$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22869735$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Banci, Lucia</creatorcontrib><creatorcontrib>Bertini, Ivano</creatorcontrib><creatorcontrib>Cantini, Francesca</creatorcontrib><creatorcontrib>Kozyreva, Tatiana</creatorcontrib><creatorcontrib>Massagni, Chiara</creatorcontrib><creatorcontrib>Palumaa, Peep</creatorcontrib><creatorcontrib>Rubino, Jeffrey T</creatorcontrib><creatorcontrib>Zovo, Kairit</creatorcontrib><title>Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Copper chaperone for superoxide dismutase 1 (SOD1), CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising one or two of the protein’s three domains. The synergy between electrospray ionization mass spectrometry (ESI-MS) and NMR is fully exploited. This is an in vitro study of this process at the molecular level. Domain 1 of hCCS is necessary to load hSOD1 with Cu(I), requiring the heterodimeric complex formation with hSOD1 fostered by the interaction with domain 2. Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57–Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.</description><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Catalysis</subject><subject>Copper</subject><subject>Copper - chemistry</subject><subject>Cysteine - chemistry</subject><subject>disulfide bonds</subject><subject>Disulfides</subject><subject>Disulfides - chemistry</subject><subject>electrospray ionization mass spectrometry</subject><subject>Humans</subject><subject>in vitro studies</subject><subject>Kinetics</subject><subject>Lyases - chemistry</subject><subject>Lyases - physiology</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Mass spectrometry</subject><subject>Molecular Chaperones - metabolism</subject><subject>Monomers</subject><subject>mutants</subject><subject>Mutation</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>nuclear magnetic resonance spectroscopy</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxygen</subject><subject>Physiology</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Spectrometry, Mass, Electrospray Ionization - methods</subject><subject>superoxide dismutase</subject><subject>Superoxide Dismutase - genetics</subject><subject>Superoxide Dismutase - physiology</subject><subject>Superoxide Dismutase-1</subject><subject>Superoxides</subject><subject>Time Factors</subject><subject>Yeasts</subject><subject>Zinc</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdks2PEyEYh4nRuLV69qSSeNk9dPd9gSlwMTH1Y0022UPdM2EYpjNNZ6gw48d_L7OtXfUCCe_DAy8_CHmJcIkg-dW-t-kSGUihOYJ-RGZ5xMVSaHhMZgBMLpRg4ow8S2kLALpQ8JScMaaWWvJiRsL12NmepnHvY_jZVp5WberGwSZPkZ4369sPeEE7O4zRDm3o6dDEMG4a2vaDj9bdr_1oh4Y29yIX9tlEXWMnYe9pHSKdJNm1Wq0vnpMntd0l_-I4z8ndp49fV9eLm9vPX1bvbxZOaDYsZIGVrzwovXRluUTONJMKytoqpR3nJedY8lphJRxT3BYaofSqKiomrHSOz8m7g3c_lp2vnO-HaHdmH9vOxl8m2Nb8W-nbxmzCd8MFk5DfZk7Oj4IYvo0-DaZrk_O7ne19GJNB4EIBqnz6nLz9D92GMfa5vXtKolAaM3V1oFwMKUVfny6DYKYwzRSmeQgz73j9dw8n_k96GaBHYNr5oNO5C4O8KCbk1QHZpiHEEyNQ5s8gIdffHOq1DcZuYpvM3ZoBLgGQaVEo_htB9bgH</recordid><startdate>20120821</startdate><enddate>20120821</enddate><creator>Banci, Lucia</creator><creator>Bertini, Ivano</creator><creator>Cantini, Francesca</creator><creator>Kozyreva, Tatiana</creator><creator>Massagni, Chiara</creator><creator>Palumaa, Peep</creator><creator>Rubino, Jeffrey T</creator><creator>Zovo, Kairit</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</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><scope>5PM</scope></search><sort><creationdate>20120821</creationdate><title>Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)</title><author>Banci, Lucia ; Bertini, Ivano ; Cantini, Francesca ; Kozyreva, Tatiana ; Massagni, Chiara ; Palumaa, Peep ; Rubino, Jeffrey T ; Zovo, Kairit</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-751dede0896cbb613292780bfa889c33b331b3f81d4c283a5910be8d5d24a7cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Catalysis</topic><topic>Copper</topic><topic>Copper - chemistry</topic><topic>Cysteine - chemistry</topic><topic>disulfide bonds</topic><topic>Disulfides</topic><topic>Disulfides - chemistry</topic><topic>electrospray ionization mass spectrometry</topic><topic>Humans</topic><topic>in vitro studies</topic><topic>Kinetics</topic><topic>Lyases - chemistry</topic><topic>Lyases - physiology</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Mass spectrometry</topic><topic>Molecular Chaperones - metabolism</topic><topic>Monomers</topic><topic>mutants</topic><topic>Mutation</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>nuclear magnetic resonance spectroscopy</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Oxygen</topic><topic>Physiology</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Spectrometry, Mass, Electrospray Ionization - methods</topic><topic>superoxide dismutase</topic><topic>Superoxide Dismutase - genetics</topic><topic>Superoxide Dismutase - physiology</topic><topic>Superoxide Dismutase-1</topic><topic>Superoxides</topic><topic>Time Factors</topic><topic>Yeasts</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Banci, Lucia</creatorcontrib><creatorcontrib>Bertini, Ivano</creatorcontrib><creatorcontrib>Cantini, Francesca</creatorcontrib><creatorcontrib>Kozyreva, Tatiana</creatorcontrib><creatorcontrib>Massagni, Chiara</creatorcontrib><creatorcontrib>Palumaa, Peep</creatorcontrib><creatorcontrib>Rubino, Jeffrey T</creatorcontrib><creatorcontrib>Zovo, Kairit</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences 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>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>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Banci, Lucia</au><au>Bertini, Ivano</au><au>Cantini, Francesca</au><au>Kozyreva, Tatiana</au><au>Massagni, Chiara</au><au>Palumaa, Peep</au><au>Rubino, Jeffrey T</au><au>Zovo, Kairit</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-08-21</date><risdate>2012</risdate><volume>109</volume><issue>34</issue><spage>13555</spage><epage>13560</epage><pages>13555-13560</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Copper chaperone for superoxide dismutase 1 (SOD1), CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising one or two of the protein’s three domains. The synergy between electrospray ionization mass spectrometry (ESI-MS) and NMR is fully exploited. This is an in vitro study of this process at the molecular level. Domain 1 of hCCS is necessary to load hSOD1 with Cu(I), requiring the heterodimeric complex formation with hSOD1 fostered by the interaction with domain 2. Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57–Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22869735</pmid><doi>10.1073/pnas.1207493109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2012-08, Vol.109 (34), p.13555-13560 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1034801828 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Binding Sites Biochemistry Biological Sciences Catalysis Copper Copper - chemistry Cysteine - chemistry disulfide bonds Disulfides Disulfides - chemistry electrospray ionization mass spectrometry Humans in vitro studies Kinetics Lyases - chemistry Lyases - physiology Magnetic Resonance Spectroscopy - methods Mass spectrometry Molecular Chaperones - metabolism Monomers mutants Mutation NMR Nuclear magnetic resonance nuclear magnetic resonance spectroscopy Oxidation Oxidation-Reduction Oxygen Physiology Protein Binding Proteins Spectrometry, Mass, Electrospray Ionization - methods superoxide dismutase Superoxide Dismutase - genetics Superoxide Dismutase - physiology Superoxide Dismutase-1 Superoxides Time Factors Yeasts Zinc |
| title | Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T22%3A36%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Human%20superoxide%20dismutase%201%20(hSOD1)%20maturation%20through%20interaction%20with%20human%20copper%20chaperone%20for%20SOD1%20(hCCS)&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Banci,%20Lucia&rft.date=2012-08-21&rft.volume=109&rft.issue=34&rft.spage=13555&rft.epage=13560&rft.pages=13555-13560&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.1207493109&rft_dat=%3Cjstor_proqu%3E41700970%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1034714891&rft_id=info:pmid/22869735&rft_jstor_id=41700970&rfr_iscdi=true |