Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A

The maturation of Escherichia coli nitrate reductase A requires the incorporation of the Mo-(bis-MGD) cofactor to the apoprotein. For this process, the NarJ chaperone is strictly required (Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., and Giordano, G. (199...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of biological chemistry 2004-10, Vol.279 (40), p.41398-41403
Hauptverfasser: Alexandra Vergnes, Kamila Gouffi-Belhabich, Francis Blasco, Gérard Giordano, Axel Magalon
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 41403
container_issue 40
container_start_page 41398
container_title The Journal of biological chemistry
container_volume 279
creator Alexandra Vergnes
Kamila Gouffi-Belhabich
Francis Blasco
Gérard Giordano
Axel Magalon
description The maturation of Escherichia coli nitrate reductase A requires the incorporation of the Mo-(bis-MGD) cofactor to the apoprotein. For this process, the NarJ chaperone is strictly required (Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., and Giordano, G. (1998) Mol. Microbiol . 28, 435–447). We report the first description of protein interactions between molybdenum cofactor biosynthetic proteins (MogA, MoeA, MobA, and MobB) and the aponitrate reductase (NarG) using a bacterial two-hybrid approach. Two conditions have to be satisfied to allow the visualization of the interactions, (i) the presence of an active and mature molybdenum cofactor and (ii) the presence of the NarJ chaperone and of the NarG structural partner subunit, NarH. Formation of tungsten-substituted cofactor prevents the interaction between NarG and the four biosynthetic proteins. Our results suggested that the final stages of molybdenum cofactor biosynthesis occur on a complex made up by MogA, MoeA, MobA, and MobB, which is also in charge with the delivery of the mature cofactor onto the aponitrate reductase A in a NarJ-assisted process.
doi_str_mv 10.1074/jbc.M407087200
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66917363</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17826457</sourcerecordid><originalsourceid>FETCH-LOGICAL-c391t-58393682ddb6d9fc7cc417753aabd25f22ae02b3d555a26aa853389981472b603</originalsourceid><addsrcrecordid>eNqFkU1v1DAQhi0EotvClSPyAXHL4o_461hWBSp1QUIgcbMcZ0JcJXGxnaIVfx5Xu6hH5jKHeeaVZh6EXlGypUS17247v923RBGtGCFP0IYSzRsu6I-naEMIo41hQp-h85xvSa3W0OfojArWKsblBv25Xu7jdA8zLAXHAZcR8D5Oh66HZZ3xLg7Ol5jw-xDzYanTEjzeOz-GBdIBh-W44cqaXAlx-Zdxlf0IKVTOYR-ngD-HUgnAX6FffXEZ8OUL9GxwU4aXp36Bvn-4-rb71Nx8-Xi9u7xpPDe0NEJzw6Vmfd_J3gxeed9SpQR3ruuZGBhzQFjHeyGEY9I5LTjXxmhab-wk4Rfo7TH3LsVfK-Ri55A9TJNbIK7ZSmmo4pL_F6RKM9kKVcHtEfQp5pxgsHcpzC4dLCX2wYutXuyjl7rw-pS8djP0j_hJRAXeHIEx_Bx_hwS2C7G-cLZMGdsS21JuNP8L5IWVgA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17826457</pqid></control><display><type>article</type><title>Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Alexandra Vergnes ; Kamila Gouffi-Belhabich ; Francis Blasco ; Gérard Giordano ; Axel Magalon</creator><creatorcontrib>Alexandra Vergnes ; Kamila Gouffi-Belhabich ; Francis Blasco ; Gérard Giordano ; Axel Magalon</creatorcontrib><description>The maturation of Escherichia coli nitrate reductase A requires the incorporation of the Mo-(bis-MGD) cofactor to the apoprotein. For this process, the NarJ chaperone is strictly required (Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., and Giordano, G. (1998) Mol. Microbiol . 28, 435–447). We report the first description of protein interactions between molybdenum cofactor biosynthetic proteins (MogA, MoeA, MobA, and MobB) and the aponitrate reductase (NarG) using a bacterial two-hybrid approach. Two conditions have to be satisfied to allow the visualization of the interactions, (i) the presence of an active and mature molybdenum cofactor and (ii) the presence of the NarJ chaperone and of the NarG structural partner subunit, NarH. Formation of tungsten-substituted cofactor prevents the interaction between NarG and the four biosynthetic proteins. Our results suggested that the final stages of molybdenum cofactor biosynthesis occur on a complex made up by MogA, MoeA, MobA, and MobB, which is also in charge with the delivery of the mature cofactor onto the aponitrate reductase A in a NarJ-assisted process.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M407087200</identifier><identifier>PMID: 15247236</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Apoproteins - metabolism ; Escherichia coli ; Escherichia coli Proteins - biosynthesis ; Escherichia coli Proteins - metabolism ; Macromolecular Substances ; Molecular Chaperones - metabolism ; Molybdenum ; Nitrate Reductase ; Nitrate Reductases - biosynthesis ; Protein Subunits - metabolism ; Sulfurtransferases - metabolism ; Trans-Activators - metabolism ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2004-10, Vol.279 (40), p.41398-41403</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-58393682ddb6d9fc7cc417753aabd25f22ae02b3d555a26aa853389981472b603</citedby><cites>FETCH-LOGICAL-c391t-58393682ddb6d9fc7cc417753aabd25f22ae02b3d555a26aa853389981472b603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15247236$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alexandra Vergnes</creatorcontrib><creatorcontrib>Kamila Gouffi-Belhabich</creatorcontrib><creatorcontrib>Francis Blasco</creatorcontrib><creatorcontrib>Gérard Giordano</creatorcontrib><creatorcontrib>Axel Magalon</creatorcontrib><title>Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The maturation of Escherichia coli nitrate reductase A requires the incorporation of the Mo-(bis-MGD) cofactor to the apoprotein. For this process, the NarJ chaperone is strictly required (Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., and Giordano, G. (1998) Mol. Microbiol . 28, 435–447). We report the first description of protein interactions between molybdenum cofactor biosynthetic proteins (MogA, MoeA, MobA, and MobB) and the aponitrate reductase (NarG) using a bacterial two-hybrid approach. Two conditions have to be satisfied to allow the visualization of the interactions, (i) the presence of an active and mature molybdenum cofactor and (ii) the presence of the NarJ chaperone and of the NarG structural partner subunit, NarH. Formation of tungsten-substituted cofactor prevents the interaction between NarG and the four biosynthetic proteins. Our results suggested that the final stages of molybdenum cofactor biosynthesis occur on a complex made up by MogA, MoeA, MobA, and MobB, which is also in charge with the delivery of the mature cofactor onto the aponitrate reductase A in a NarJ-assisted process.</description><subject>Apoproteins - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - biosynthesis</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Macromolecular Substances</subject><subject>Molecular Chaperones - metabolism</subject><subject>Molybdenum</subject><subject>Nitrate Reductase</subject><subject>Nitrate Reductases - biosynthesis</subject><subject>Protein Subunits - metabolism</subject><subject>Sulfurtransferases - metabolism</subject><subject>Trans-Activators - metabolism</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EotvClSPyAXHL4o_461hWBSp1QUIgcbMcZ0JcJXGxnaIVfx5Xu6hH5jKHeeaVZh6EXlGypUS17247v923RBGtGCFP0IYSzRsu6I-naEMIo41hQp-h85xvSa3W0OfojArWKsblBv25Xu7jdA8zLAXHAZcR8D5Oh66HZZ3xLg7Ol5jw-xDzYanTEjzeOz-GBdIBh-W44cqaXAlx-Zdxlf0IKVTOYR-ngD-HUgnAX6FffXEZ8OUL9GxwU4aXp36Bvn-4-rb71Nx8-Xi9u7xpPDe0NEJzw6Vmfd_J3gxeed9SpQR3ruuZGBhzQFjHeyGEY9I5LTjXxmhab-wk4Rfo7TH3LsVfK-Ri55A9TJNbIK7ZSmmo4pL_F6RKM9kKVcHtEfQp5pxgsHcpzC4dLCX2wYutXuyjl7rw-pS8djP0j_hJRAXeHIEx_Bx_hwS2C7G-cLZMGdsS21JuNP8L5IWVgA</recordid><startdate>20041001</startdate><enddate>20041001</enddate><creator>Alexandra Vergnes</creator><creator>Kamila Gouffi-Belhabich</creator><creator>Francis Blasco</creator><creator>Gérard Giordano</creator><creator>Axel Magalon</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20041001</creationdate><title>Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A</title><author>Alexandra Vergnes ; Kamila Gouffi-Belhabich ; Francis Blasco ; Gérard Giordano ; Axel Magalon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-58393682ddb6d9fc7cc417753aabd25f22ae02b3d555a26aa853389981472b603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Apoproteins - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - biosynthesis</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Macromolecular Substances</topic><topic>Molecular Chaperones - metabolism</topic><topic>Molybdenum</topic><topic>Nitrate Reductase</topic><topic>Nitrate Reductases - biosynthesis</topic><topic>Protein Subunits - metabolism</topic><topic>Sulfurtransferases - metabolism</topic><topic>Trans-Activators - metabolism</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alexandra Vergnes</creatorcontrib><creatorcontrib>Kamila Gouffi-Belhabich</creatorcontrib><creatorcontrib>Francis Blasco</creatorcontrib><creatorcontrib>Gérard Giordano</creatorcontrib><creatorcontrib>Axel Magalon</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alexandra Vergnes</au><au>Kamila Gouffi-Belhabich</au><au>Francis Blasco</au><au>Gérard Giordano</au><au>Axel Magalon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-10-01</date><risdate>2004</risdate><volume>279</volume><issue>40</issue><spage>41398</spage><epage>41403</epage><pages>41398-41403</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The maturation of Escherichia coli nitrate reductase A requires the incorporation of the Mo-(bis-MGD) cofactor to the apoprotein. For this process, the NarJ chaperone is strictly required (Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., and Giordano, G. (1998) Mol. Microbiol . 28, 435–447). We report the first description of protein interactions between molybdenum cofactor biosynthetic proteins (MogA, MoeA, MobA, and MobB) and the aponitrate reductase (NarG) using a bacterial two-hybrid approach. Two conditions have to be satisfied to allow the visualization of the interactions, (i) the presence of an active and mature molybdenum cofactor and (ii) the presence of the NarJ chaperone and of the NarG structural partner subunit, NarH. Formation of tungsten-substituted cofactor prevents the interaction between NarG and the four biosynthetic proteins. Our results suggested that the final stages of molybdenum cofactor biosynthesis occur on a complex made up by MogA, MoeA, MobA, and MobB, which is also in charge with the delivery of the mature cofactor onto the aponitrate reductase A in a NarJ-assisted process.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15247236</pmid><doi>10.1074/jbc.M407087200</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 2004-10, Vol.279 (40), p.41398-41403
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_66917363
source MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects Apoproteins - metabolism
Escherichia coli
Escherichia coli Proteins - biosynthesis
Escherichia coli Proteins - metabolism
Macromolecular Substances
Molecular Chaperones - metabolism
Molybdenum
Nitrate Reductase
Nitrate Reductases - biosynthesis
Protein Subunits - metabolism
Sulfurtransferases - metabolism
Trans-Activators - metabolism
Two-Hybrid System Techniques
title Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T20%3A09%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Involvement%20of%20the%20Molybdenum%20Cofactor%20Biosynthetic%20Machinery%20in%20the%20Maturation%20of%20the%20Escherichia%20coli%20Nitrate%20Reductase%20A&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Alexandra%20Vergnes&rft.date=2004-10-01&rft.volume=279&rft.issue=40&rft.spage=41398&rft.epage=41403&rft.pages=41398-41403&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M407087200&rft_dat=%3Cproquest_cross%3E17826457%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17826457&rft_id=info:pmid/15247236&rfr_iscdi=true