Molecular characterization of the heteromeric coenzyme A-synthesizing protein complex (CoA-SPC) in the yeast Saccharomyces cerevisiae
Abstract Coenzyme A (CoA) as an essential cofactor for acyl and acetyl transfer reactions is synthesized in five enzymatic steps from pantothenate, cysteine, and ATP. In the yeast Saccharomyces cerevisiae, products of five essential genes CAB1-CAB5 (coenzyme A biosynthesis) are required to catalyze...
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| Veröffentlicht in: | FEMS yeast research 2013-09, Vol.13 (6), p.565-573 |
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| creator | Olzhausen, Judith Moritz, Tom Neetz, Tim Schüller, Hans-Joachim |
| description | Abstract
Coenzyme A (CoA) as an essential cofactor for acyl and acetyl transfer reactions is synthesized in five enzymatic steps from pantothenate, cysteine, and ATP. In the yeast Saccharomyces cerevisiae, products of five essential genes CAB1-CAB5 (coenzyme A biosynthesis) are required to catalyze CoA biosynthesis. In addition, nonessential genes SIS2 and VHS3 similar to CAB3 are also involved. Using epitope-tagged variants of Cab3 and Cab5, we show that both proteins cofractionate upon chromatographic separation, forming a complex of about 330 kDa. We thus systematically investigated interactions among Cab proteins. Our results show that Cab2, Cab3, Cab4, and Cab5 indeed bind to each other, with Cab3 as the sole protein, which can interact with itself and other Cab proteins. Cab3 also binds to Sis2 and Vhs3 that were previously characterized as subunits of phosphopantothenoylcysteine decarboxylase. Pantothenate kinase encoded by CAB1 as the rate-limiting enzyme of CoA biosynthesis did not interact with other Cab proteins. Mapping studies revealed that the nonconserved N-terminus of Cab3 is required for dimerization and for binding of Cab2 and Cab5. Our interaction studies confirm early reports on the existence of a CoA-synthesizing protein complex (CoA-SPC) in yeast and provide precise data on protein domains involved in complex formation. |
| doi_str_mv | 10.1111/1567-1364.12058 |
| format | Article |
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Coenzyme A (CoA) as an essential cofactor for acyl and acetyl transfer reactions is synthesized in five enzymatic steps from pantothenate, cysteine, and ATP. In the yeast Saccharomyces cerevisiae, products of five essential genes CAB1-CAB5 (coenzyme A biosynthesis) are required to catalyze CoA biosynthesis. In addition, nonessential genes SIS2 and VHS3 similar to CAB3 are also involved. Using epitope-tagged variants of Cab3 and Cab5, we show that both proteins cofractionate upon chromatographic separation, forming a complex of about 330 kDa. We thus systematically investigated interactions among Cab proteins. Our results show that Cab2, Cab3, Cab4, and Cab5 indeed bind to each other, with Cab3 as the sole protein, which can interact with itself and other Cab proteins. Cab3 also binds to Sis2 and Vhs3 that were previously characterized as subunits of phosphopantothenoylcysteine decarboxylase. Pantothenate kinase encoded by CAB1 as the rate-limiting enzyme of CoA biosynthesis did not interact with other Cab proteins. Mapping studies revealed that the nonconserved N-terminus of Cab3 is required for dimerization and for binding of Cab2 and Cab5. Our interaction studies confirm early reports on the existence of a CoA-synthesizing protein complex (CoA-SPC) in yeast and provide precise data on protein domains involved in complex formation.</description><identifier>ISSN: 1567-1356</identifier><identifier>EISSN: 1567-1364</identifier><identifier>DOI: 10.1111/1567-1364.12058</identifier><identifier>PMID: 23789928</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>ATP ; Biosynthesis ; Biosynthetic Pathways ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Coenzyme A ; Coenzyme A - biosynthesis ; Dimerization ; Kinases ; Molecular Weight ; multienzyme complex ; Multienzyme Complexes - chemistry ; Multienzyme Complexes - genetics ; Multienzyme Complexes - isolation & purification ; Multienzyme Complexes - metabolism ; N-Terminus ; Pantothenate kinase ; Peptide mapping ; Phosphopantothenoylcysteine decarboxylase ; Protein Binding ; Protein Interaction Mapping ; Protein Multimerization ; Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Yeast</subject><ispartof>FEMS yeast research, 2013-09, Vol.13 (6), p.565-573</ispartof><rights>2013 Federation of European Microbiological Societies Published by John Wiley & Sons Ltd. All rights reserved 2013</rights><rights>2013 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved</rights><rights>2013 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved.</rights><rights>2013 Federation of European Microbiological Societies Published by John Wiley & Sons Ltd. All rights reserved</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4398-3a3aeed094e09ae8875995e6e4e97792842c69c62b76f289f31b900a3fb8e0133</citedby><cites>FETCH-LOGICAL-c4398-3a3aeed094e09ae8875995e6e4e97792842c69c62b76f289f31b900a3fb8e0133</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%2F1567-1364.12058$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1567-1364.12058$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23789928$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Olzhausen, Judith</creatorcontrib><creatorcontrib>Moritz, Tom</creatorcontrib><creatorcontrib>Neetz, Tim</creatorcontrib><creatorcontrib>Schüller, Hans-Joachim</creatorcontrib><title>Molecular characterization of the heteromeric coenzyme A-synthesizing protein complex (CoA-SPC) in the yeast Saccharomyces cerevisiae</title><title>FEMS yeast research</title><addtitle>FEMS Yeast Res</addtitle><description>Abstract
Coenzyme A (CoA) as an essential cofactor for acyl and acetyl transfer reactions is synthesized in five enzymatic steps from pantothenate, cysteine, and ATP. In the yeast Saccharomyces cerevisiae, products of five essential genes CAB1-CAB5 (coenzyme A biosynthesis) are required to catalyze CoA biosynthesis. In addition, nonessential genes SIS2 and VHS3 similar to CAB3 are also involved. Using epitope-tagged variants of Cab3 and Cab5, we show that both proteins cofractionate upon chromatographic separation, forming a complex of about 330 kDa. We thus systematically investigated interactions among Cab proteins. Our results show that Cab2, Cab3, Cab4, and Cab5 indeed bind to each other, with Cab3 as the sole protein, which can interact with itself and other Cab proteins. Cab3 also binds to Sis2 and Vhs3 that were previously characterized as subunits of phosphopantothenoylcysteine decarboxylase. Pantothenate kinase encoded by CAB1 as the rate-limiting enzyme of CoA biosynthesis did not interact with other Cab proteins. Mapping studies revealed that the nonconserved N-terminus of Cab3 is required for dimerization and for binding of Cab2 and Cab5. Our interaction studies confirm early reports on the existence of a CoA-synthesizing protein complex (CoA-SPC) in yeast and provide precise data on protein domains involved in complex formation.</description><subject>ATP</subject><subject>Biosynthesis</subject><subject>Biosynthetic Pathways</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Coenzyme A</subject><subject>Coenzyme A - biosynthesis</subject><subject>Dimerization</subject><subject>Kinases</subject><subject>Molecular Weight</subject><subject>multienzyme complex</subject><subject>Multienzyme Complexes - chemistry</subject><subject>Multienzyme Complexes - genetics</subject><subject>Multienzyme Complexes - isolation & purification</subject><subject>Multienzyme Complexes - metabolism</subject><subject>N-Terminus</subject><subject>Pantothenate kinase</subject><subject>Peptide mapping</subject><subject>Phosphopantothenoylcysteine decarboxylase</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Yeast</subject><issn>1567-1356</issn><issn>1567-1364</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkUtr3DAUhUVpaB7tursi6GYScKKXbWk5DM0DElKadtGV0CjXHQXbmkh2Gs8-_ztyJhlCKbTaSBx99-heHYQ-UnJI0zqieVFmlBfikDKSyzdoZ6O83ZzzYhvtxnhDCC0Jke_QNuOlVIrJHfRw4WuwfW0CtgsTjO0guJXpnG-xr3C3ALyApPkm6RZbD-1qaABPszi06Ta6lWt_4WXwHbg23TfLGu7xZOan2dXX2T5O4mgygIkdvjJ2fMU3g4WILQS4c9EZeI-2KlNH-PC876Efx1--z06z88uTs9n0PLOCK5lxww3ANVECiDIgZZkrlUMBAlRZpnkEs4WyBZuXRcWkqjidK0IMr-YSCOV8D03Wvqnf2x5ipxsXLdS1acH3UVMhOE9_xMh_oFRxwfJCJPTzH-iN70ObBtGMc1FyJpRM1NGassHHGKDSy-AaEwZNiR7D1GNceoxOP4WZKj49-_bzBq43_Et6CcjXwG9Xw_AvP33889uL8cG6zvfLv1Zlr7p4BLFvtTI</recordid><startdate>20130901</startdate><enddate>20130901</enddate><creator>Olzhausen, Judith</creator><creator>Moritz, Tom</creator><creator>Neetz, Tim</creator><creator>Schüller, Hans-Joachim</creator><general>Blackwell Publishing Ltd</general><general>Oxford University Press</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>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>M7N</scope></search><sort><creationdate>20130901</creationdate><title>Molecular characterization of the heteromeric coenzyme A-synthesizing protein complex (CoA-SPC) in the yeast Saccharomyces cerevisiae</title><author>Olzhausen, Judith ; Moritz, Tom ; Neetz, Tim ; Schüller, Hans-Joachim</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4398-3a3aeed094e09ae8875995e6e4e97792842c69c62b76f289f31b900a3fb8e0133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>ATP</topic><topic>Biosynthesis</topic><topic>Biosynthetic Pathways</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Coenzyme A</topic><topic>Coenzyme A - biosynthesis</topic><topic>Dimerization</topic><topic>Kinases</topic><topic>Molecular Weight</topic><topic>multienzyme complex</topic><topic>Multienzyme Complexes - chemistry</topic><topic>Multienzyme Complexes - genetics</topic><topic>Multienzyme Complexes - isolation & purification</topic><topic>Multienzyme Complexes - metabolism</topic><topic>N-Terminus</topic><topic>Pantothenate kinase</topic><topic>Peptide mapping</topic><topic>Phosphopantothenoylcysteine decarboxylase</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olzhausen, Judith</creatorcontrib><creatorcontrib>Moritz, Tom</creatorcontrib><creatorcontrib>Neetz, Tim</creatorcontrib><creatorcontrib>Schüller, Hans-Joachim</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science 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>MEDLINE - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>FEMS yeast research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Olzhausen, Judith</au><au>Moritz, Tom</au><au>Neetz, Tim</au><au>Schüller, Hans-Joachim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization of the heteromeric coenzyme A-synthesizing protein complex (CoA-SPC) in the yeast Saccharomyces cerevisiae</atitle><jtitle>FEMS yeast research</jtitle><addtitle>FEMS Yeast Res</addtitle><date>2013-09-01</date><risdate>2013</risdate><volume>13</volume><issue>6</issue><spage>565</spage><epage>573</epage><pages>565-573</pages><issn>1567-1356</issn><eissn>1567-1364</eissn><abstract>Abstract
Coenzyme A (CoA) as an essential cofactor for acyl and acetyl transfer reactions is synthesized in five enzymatic steps from pantothenate, cysteine, and ATP. In the yeast Saccharomyces cerevisiae, products of five essential genes CAB1-CAB5 (coenzyme A biosynthesis) are required to catalyze CoA biosynthesis. In addition, nonessential genes SIS2 and VHS3 similar to CAB3 are also involved. Using epitope-tagged variants of Cab3 and Cab5, we show that both proteins cofractionate upon chromatographic separation, forming a complex of about 330 kDa. We thus systematically investigated interactions among Cab proteins. Our results show that Cab2, Cab3, Cab4, and Cab5 indeed bind to each other, with Cab3 as the sole protein, which can interact with itself and other Cab proteins. Cab3 also binds to Sis2 and Vhs3 that were previously characterized as subunits of phosphopantothenoylcysteine decarboxylase. Pantothenate kinase encoded by CAB1 as the rate-limiting enzyme of CoA biosynthesis did not interact with other Cab proteins. Mapping studies revealed that the nonconserved N-terminus of Cab3 is required for dimerization and for binding of Cab2 and Cab5. Our interaction studies confirm early reports on the existence of a CoA-synthesizing protein complex (CoA-SPC) in yeast and provide precise data on protein domains involved in complex formation.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>23789928</pmid><doi>10.1111/1567-1364.12058</doi><tpages>9</tpages></addata></record> |
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| subjects | ATP Biosynthesis Biosynthetic Pathways Carrier Proteins - genetics Carrier Proteins - metabolism Coenzyme A Coenzyme A - biosynthesis Dimerization Kinases Molecular Weight multienzyme complex Multienzyme Complexes - chemistry Multienzyme Complexes - genetics Multienzyme Complexes - isolation & purification Multienzyme Complexes - metabolism N-Terminus Pantothenate kinase Peptide mapping Phosphopantothenoylcysteine decarboxylase Protein Binding Protein Interaction Mapping Protein Multimerization Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Yeast |
| title | Molecular characterization of the heteromeric coenzyme A-synthesizing protein complex (CoA-SPC) in the yeast Saccharomyces cerevisiae |
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