Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation
Chaperone proteins that traffic copper around the cell minimise its toxicity by maintaining it in a tightly bound form. The transfer of copper from chaperones to target proteins is promoted by complex formation, but the kinetic characteristics of transfer have yet to be demonstrated for any chaperon...
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2017, Vol.53 (8), p.1397-1400 |
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| container_title | Chemical communications (Cambridge, England) |
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| creator | Kay, Kristine L Zhou, Liang Tenori, Leonardo Bradley, Justin M Singleton, Chloe Kihlken, Margaret A Ciofi-Baffoni, Simone Le Brun, Nick E |
| description | Chaperone proteins that traffic copper around the cell minimise its toxicity by maintaining it in a tightly bound form. The transfer of copper from chaperones to target proteins is promoted by complex formation, but the kinetic characteristics of transfer have yet to be demonstrated for any chaperone-target protein pair. Here we report studies of copper transfer between the Atx1-type chaperone CopZ from Bacillus subtilis and the soluble domains of its cognate P-type ATPase transporter, CopAab. Transfer of copper from CopZ to CopAab was found to occur rapidly, with a rate constant at 25 °C of ∼267 s
, many orders of magnitude higher than that for Cu(i) dissociation from CopZ in the absence of CopAab. The data demonstrate that complex formation between CopZ and CopAab, evidence for which is provided by NMR and electrospray ionisation mass spectrometry, dramatically enhances the rate of Cu(i) dissociation from CopZ. |
| doi_str_mv | 10.1039/c6cc08966f |
| format | Article |
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, many orders of magnitude higher than that for Cu(i) dissociation from CopZ in the absence of CopAab. The data demonstrate that complex formation between CopZ and CopAab, evidence for which is provided by NMR and electrospray ionisation mass spectrometry, dramatically enhances the rate of Cu(i) dissociation from CopZ.</description><subject>Complex formation</subject><subject>Copper</subject><subject>Ionization</subject><subject>Mass spectrometry</subject><subject>Proteins</subject><subject>Rate constants</subject><subject>Toxicity</subject><subject>Transporter</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNo9kEtLxDAUhYMoPkY3_gDJUoRqMnm1SymOigNuFNyVNL1xIm1Tkww4_96Mjt7NPRw-DvcehM4puaaEVTdGGkPKSkq7h44pk7wQvHzb32pRFYpxcYROYvwgeagoD9HRvCSqZJwfo9WTGyE5g_Wo-010EXuLjZ8mCDgFPUabhQ1-wBqblc62HwEnj12KOOnwDglPwSdwIx6gczpBh9tNjhimHr6w9WHQyfnxFB1Y3Uc42-0Zel3cvdQPxfL5_rG-XRaGCZmK1mhDK961TLHS0nllhBWW2q7KrlRd23bQClUKAZoSqrkxwLWQgikOlSZshi5_c_NVn2uIqRlcNND3egS_jg0tVZVHCJXRq1_UBB9jANtMwQ06bBpKmm2zTS3r-qfZRYYvdrnrNj_6j_5Vyb4BYP91uw</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Kay, Kristine L</creator><creator>Zhou, Liang</creator><creator>Tenori, Leonardo</creator><creator>Bradley, Justin M</creator><creator>Singleton, Chloe</creator><creator>Kihlken, Margaret A</creator><creator>Ciofi-Baffoni, Simone</creator><creator>Le Brun, Nick E</creator><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0001-9780-4061</orcidid></search><sort><creationdate>2017</creationdate><title>Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation</title><author>Kay, Kristine L ; Zhou, Liang ; Tenori, Leonardo ; Bradley, Justin M ; Singleton, Chloe ; Kihlken, Margaret A ; Ciofi-Baffoni, Simone ; Le Brun, Nick E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-bcac194db3738f129c5f5f1fd919467dbbdeb57855ea101a4cce4a565374e9a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Complex formation</topic><topic>Copper</topic><topic>Ionization</topic><topic>Mass spectrometry</topic><topic>Proteins</topic><topic>Rate constants</topic><topic>Toxicity</topic><topic>Transporter</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kay, Kristine L</creatorcontrib><creatorcontrib>Zhou, Liang</creatorcontrib><creatorcontrib>Tenori, Leonardo</creatorcontrib><creatorcontrib>Bradley, Justin M</creatorcontrib><creatorcontrib>Singleton, Chloe</creatorcontrib><creatorcontrib>Kihlken, Margaret A</creatorcontrib><creatorcontrib>Ciofi-Baffoni, Simone</creatorcontrib><creatorcontrib>Le Brun, Nick E</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kay, Kristine L</au><au>Zhou, Liang</au><au>Tenori, Leonardo</au><au>Bradley, Justin M</au><au>Singleton, Chloe</au><au>Kihlken, Margaret A</au><au>Ciofi-Baffoni, Simone</au><au>Le Brun, Nick E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2017</date><risdate>2017</risdate><volume>53</volume><issue>8</issue><spage>1397</spage><epage>1400</epage><pages>1397-1400</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Chaperone proteins that traffic copper around the cell minimise its toxicity by maintaining it in a tightly bound form. The transfer of copper from chaperones to target proteins is promoted by complex formation, but the kinetic characteristics of transfer have yet to be demonstrated for any chaperone-target protein pair. Here we report studies of copper transfer between the Atx1-type chaperone CopZ from Bacillus subtilis and the soluble domains of its cognate P-type ATPase transporter, CopAab. Transfer of copper from CopZ to CopAab was found to occur rapidly, with a rate constant at 25 °C of ∼267 s
, many orders of magnitude higher than that for Cu(i) dissociation from CopZ in the absence of CopAab. The data demonstrate that complex formation between CopZ and CopAab, evidence for which is provided by NMR and electrospray ionisation mass spectrometry, dramatically enhances the rate of Cu(i) dissociation from CopZ.</abstract><cop>England</cop><pmid>28078344</pmid><doi>10.1039/c6cc08966f</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0001-9780-4061</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Chemical communications (Cambridge, England), 2017, Vol.53 (8), p.1397-1400 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_1879999557 |
| source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Complex formation Copper Ionization Mass spectrometry Proteins Rate constants Toxicity Transporter |
| title | Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation |
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