Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase
We report structural and functional analyses of the Bradyrhizobium japonicum fixGHIS genes, which map immediately downstream of the fixNOQP operon for the symbiotically essential cbb3-type heme-copper oxidase complex. Expression of fixGHIS, like that of fixNOQP, is strongly induced in cells grown mi...
Gespeichert in:
Veröffentlicht in: | Archives of microbiology 1996-05, Vol.165 (5), p.297-305 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 305 |
---|---|
container_issue | 5 |
container_start_page | 297 |
container_title | Archives of microbiology |
container_volume | 165 |
creator | Preisig, O Zufferey, R Hannecke, H |
description | We report structural and functional analyses of the Bradyrhizobium japonicum fixGHIS genes, which map immediately downstream of the fixNOQP operon for the symbiotically essential cbb3-type heme-copper oxidase complex. Expression of fixGHIS, like that of fixNOQP, is strongly induced in cells grown microaerobically or aerobically. A fixGHI deletion led to the same prominent phenotypes as those known from a fixNOQP deletion: defective symbiotic nitrogen fixation (Fix-) and decreased cytochrome oxidase activity in cells grown under oxygen deprivation. Only traces, if any, of cytochrome cbb3 subunits were present in membranes isolated from the delta fixGHI strain, as revealed by Western blot analysis with subunit-specific antibodies. This effect was not due to lack of fixNOQP transcription. The results suggested a critical involvement of the fixGHIS gene products in the assembly and/or stability of the cbb3-type heme-copper oxidase. On the basis of sequence similarities between the FixI protein and a Cu-transporting P-type ATPase (CopA) of Enterococcus hirae, and between FixG and a membrane-bound oxidoreductase (RdxA) of Rhodobacter sphaeroides, we postulate that a membrane-bound FixGHIS complex might play a role in uptake and metabolism of copper required for the cbb3-type heme-copper oxidase. |
doi_str_mv | 10.1007/s002030050330 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_78069913</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>78069913</sourcerecordid><originalsourceid>FETCH-LOGICAL-f174t-ae56075e22f41186434014a53ecd12a13d2c04b8b9457a53ba76ecbd9250e1f03</originalsourceid><addsrcrecordid>eNo9kc1r3DAQxUVpSTdpjz2W6lByczv6sC0fm5AvCOSQBnozY3m0VlhbG8mmcf_6qM3S0xve-zEMbxj7JOCbAKi_JwAJCqAEpeAN2witZAG1_PWWbbIvC9Mo9Z4dp_QIIKQx5ogdmaoSjYQN-30WsV_j4P-Ezi8jf8R9mLzNk_PPV9c393xLEyWOkXikp8VH6rkLkc8D_dURZx8mHtw_Y_DboUDn_OTnlduuU8W87onbdQ52iGEkHp59j4k-sHcOd4k-HvSEPVxe_Dy_Lm7vrm7Of9wWTtR6LpDKCuqSpHRaCFNppUFoLBXZXkgUqpcWdGe6Rpd1tjusK7Jd38gSSDhQJ-z0de8-hqeF0tyOPlna7XCisKS2NlA1jVAZ_HwAl26kvt1HP2Jc20NTOf96yDFZ3LmIk_XpP6bylQZ0xr68Yg5Di9uYkYd7CUKBKGX-VKVeAIHmgRA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>78069913</pqid></control><display><type>article</type><title>Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase</title><source>MEDLINE</source><source>Springer Journals</source><creator>Preisig, O ; Zufferey, R ; Hannecke, H</creator><creatorcontrib>Preisig, O ; Zufferey, R ; Hannecke, H</creatorcontrib><description>We report structural and functional analyses of the Bradyrhizobium japonicum fixGHIS genes, which map immediately downstream of the fixNOQP operon for the symbiotically essential cbb3-type heme-copper oxidase complex. Expression of fixGHIS, like that of fixNOQP, is strongly induced in cells grown microaerobically or aerobically. A fixGHI deletion led to the same prominent phenotypes as those known from a fixNOQP deletion: defective symbiotic nitrogen fixation (Fix-) and decreased cytochrome oxidase activity in cells grown under oxygen deprivation. Only traces, if any, of cytochrome cbb3 subunits were present in membranes isolated from the delta fixGHI strain, as revealed by Western blot analysis with subunit-specific antibodies. This effect was not due to lack of fixNOQP transcription. The results suggested a critical involvement of the fixGHIS gene products in the assembly and/or stability of the cbb3-type heme-copper oxidase. On the basis of sequence similarities between the FixI protein and a Cu-transporting P-type ATPase (CopA) of Enterococcus hirae, and between FixG and a membrane-bound oxidoreductase (RdxA) of Rhodobacter sphaeroides, we postulate that a membrane-bound FixGHIS complex might play a role in uptake and metabolism of copper required for the cbb3-type heme-copper oxidase.</description><identifier>ISSN: 0302-8933</identifier><identifier>EISSN: 1432-072X</identifier><identifier>DOI: 10.1007/s002030050330</identifier><identifier>PMID: 8661920</identifier><identifier>CODEN: AMICCW</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Amino Acid Sequence ; amino acid sequences ; bacterial proteins ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Blotting, Western ; Bradyrhizobium japonicum ; cell membranes ; Chromosome Mapping ; Cloning, Molecular ; comparisons ; Copper - metabolism ; cytochrome-c oxidase ; deletions ; DNA Primers ; Electron Transport Complex IV - biosynthesis ; Electron Transport Complex IV - chemistry ; Electron Transport Complex IV - genetics ; fix proteins ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial - genetics ; Genetics ; heme copper oxidase complex ; ion transport ; membrane proteins ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Microbiology ; Molecular Sequence Data ; Mutation - genetics ; nitrogen fixation ; Operon - genetics ; Oxygen - pharmacology ; Rhizobiaceae - enzymology ; Rhizobiaceae - genetics ; Sequence Alignment ; Sequence Analysis ; structural genes ; structure-activity relationships ; symbiosis ; transcription (genetics) ; Transcription, Genetic</subject><ispartof>Archives of microbiology, 1996-05, Vol.165 (5), p.297-305</ispartof><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3075804$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8661920$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Preisig, O</creatorcontrib><creatorcontrib>Zufferey, R</creatorcontrib><creatorcontrib>Hannecke, H</creatorcontrib><title>Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase</title><title>Archives of microbiology</title><addtitle>Arch Microbiol</addtitle><description>We report structural and functional analyses of the Bradyrhizobium japonicum fixGHIS genes, which map immediately downstream of the fixNOQP operon for the symbiotically essential cbb3-type heme-copper oxidase complex. Expression of fixGHIS, like that of fixNOQP, is strongly induced in cells grown microaerobically or aerobically. A fixGHI deletion led to the same prominent phenotypes as those known from a fixNOQP deletion: defective symbiotic nitrogen fixation (Fix-) and decreased cytochrome oxidase activity in cells grown under oxygen deprivation. Only traces, if any, of cytochrome cbb3 subunits were present in membranes isolated from the delta fixGHI strain, as revealed by Western blot analysis with subunit-specific antibodies. This effect was not due to lack of fixNOQP transcription. The results suggested a critical involvement of the fixGHIS gene products in the assembly and/or stability of the cbb3-type heme-copper oxidase. On the basis of sequence similarities between the FixI protein and a Cu-transporting P-type ATPase (CopA) of Enterococcus hirae, and between FixG and a membrane-bound oxidoreductase (RdxA) of Rhodobacter sphaeroides, we postulate that a membrane-bound FixGHIS complex might play a role in uptake and metabolism of copper required for the cbb3-type heme-copper oxidase.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>bacterial proteins</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Bradyrhizobium japonicum</subject><subject>cell membranes</subject><subject>Chromosome Mapping</subject><subject>Cloning, Molecular</subject><subject>comparisons</subject><subject>Copper - metabolism</subject><subject>cytochrome-c oxidase</subject><subject>deletions</subject><subject>DNA Primers</subject><subject>Electron Transport Complex IV - biosynthesis</subject><subject>Electron Transport Complex IV - chemistry</subject><subject>Electron Transport Complex IV - genetics</subject><subject>fix proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial - genetics</subject><subject>Genetics</subject><subject>heme copper oxidase complex</subject><subject>ion transport</subject><subject>membrane proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>nitrogen fixation</subject><subject>Operon - genetics</subject><subject>Oxygen - pharmacology</subject><subject>Rhizobiaceae - enzymology</subject><subject>Rhizobiaceae - genetics</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis</subject><subject>structural genes</subject><subject>structure-activity relationships</subject><subject>symbiosis</subject><subject>transcription (genetics)</subject><subject>Transcription, Genetic</subject><issn>0302-8933</issn><issn>1432-072X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kc1r3DAQxUVpSTdpjz2W6lByczv6sC0fm5AvCOSQBnozY3m0VlhbG8mmcf_6qM3S0xve-zEMbxj7JOCbAKi_JwAJCqAEpeAN2witZAG1_PWWbbIvC9Mo9Z4dp_QIIKQx5ogdmaoSjYQN-30WsV_j4P-Ezi8jf8R9mLzNk_PPV9c393xLEyWOkXikp8VH6rkLkc8D_dURZx8mHtw_Y_DboUDn_OTnlduuU8W87onbdQ52iGEkHp59j4k-sHcOd4k-HvSEPVxe_Dy_Lm7vrm7Of9wWTtR6LpDKCuqSpHRaCFNppUFoLBXZXkgUqpcWdGe6Rpd1tjusK7Jd38gSSDhQJ-z0de8-hqeF0tyOPlna7XCisKS2NlA1jVAZ_HwAl26kvt1HP2Jc20NTOf96yDFZ3LmIk_XpP6bylQZ0xr68Yg5Di9uYkYd7CUKBKGX-VKVeAIHmgRA</recordid><startdate>199605</startdate><enddate>199605</enddate><creator>Preisig, O</creator><creator>Zufferey, R</creator><creator>Hannecke, H</creator><general>Springer</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>199605</creationdate><title>Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase</title><author>Preisig, O ; Zufferey, R ; Hannecke, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f174t-ae56075e22f41186434014a53ecd12a13d2c04b8b9457a53ba76ecbd9250e1f03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>bacterial proteins</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Bradyrhizobium japonicum</topic><topic>cell membranes</topic><topic>Chromosome Mapping</topic><topic>Cloning, Molecular</topic><topic>comparisons</topic><topic>Copper - metabolism</topic><topic>cytochrome-c oxidase</topic><topic>deletions</topic><topic>DNA Primers</topic><topic>Electron Transport Complex IV - biosynthesis</topic><topic>Electron Transport Complex IV - chemistry</topic><topic>Electron Transport Complex IV - genetics</topic><topic>fix proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial - genetics</topic><topic>Genetics</topic><topic>heme copper oxidase complex</topic><topic>ion transport</topic><topic>membrane proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Mutation - genetics</topic><topic>nitrogen fixation</topic><topic>Operon - genetics</topic><topic>Oxygen - pharmacology</topic><topic>Rhizobiaceae - enzymology</topic><topic>Rhizobiaceae - genetics</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis</topic><topic>structural genes</topic><topic>structure-activity relationships</topic><topic>symbiosis</topic><topic>transcription (genetics)</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Preisig, O</creatorcontrib><creatorcontrib>Zufferey, R</creatorcontrib><creatorcontrib>Hannecke, H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Preisig, O</au><au>Zufferey, R</au><au>Hannecke, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase</atitle><jtitle>Archives of microbiology</jtitle><addtitle>Arch Microbiol</addtitle><date>1996-05</date><risdate>1996</risdate><volume>165</volume><issue>5</issue><spage>297</spage><epage>305</epage><pages>297-305</pages><issn>0302-8933</issn><eissn>1432-072X</eissn><coden>AMICCW</coden><abstract>We report structural and functional analyses of the Bradyrhizobium japonicum fixGHIS genes, which map immediately downstream of the fixNOQP operon for the symbiotically essential cbb3-type heme-copper oxidase complex. Expression of fixGHIS, like that of fixNOQP, is strongly induced in cells grown microaerobically or aerobically. A fixGHI deletion led to the same prominent phenotypes as those known from a fixNOQP deletion: defective symbiotic nitrogen fixation (Fix-) and decreased cytochrome oxidase activity in cells grown under oxygen deprivation. Only traces, if any, of cytochrome cbb3 subunits were present in membranes isolated from the delta fixGHI strain, as revealed by Western blot analysis with subunit-specific antibodies. This effect was not due to lack of fixNOQP transcription. The results suggested a critical involvement of the fixGHIS gene products in the assembly and/or stability of the cbb3-type heme-copper oxidase. On the basis of sequence similarities between the FixI protein and a Cu-transporting P-type ATPase (CopA) of Enterococcus hirae, and between FixG and a membrane-bound oxidoreductase (RdxA) of Rhodobacter sphaeroides, we postulate that a membrane-bound FixGHIS complex might play a role in uptake and metabolism of copper required for the cbb3-type heme-copper oxidase.</abstract><cop>Heidelberg</cop><cop>Berlin</cop><pub>Springer</pub><pmid>8661920</pmid><doi>10.1007/s002030050330</doi><tpages>9</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0302-8933 |
ispartof | Archives of microbiology, 1996-05, Vol.165 (5), p.297-305 |
issn | 0302-8933 1432-072X |
language | eng |
recordid | cdi_proquest_miscellaneous_78069913 |
source | MEDLINE; Springer Journals |
subjects | Amino Acid Sequence amino acid sequences bacterial proteins Bacteriology Base Sequence Biological and medical sciences Blotting, Western Bradyrhizobium japonicum cell membranes Chromosome Mapping Cloning, Molecular comparisons Copper - metabolism cytochrome-c oxidase deletions DNA Primers Electron Transport Complex IV - biosynthesis Electron Transport Complex IV - chemistry Electron Transport Complex IV - genetics fix proteins Fundamental and applied biological sciences. Psychology Genes, Bacterial - genetics Genetics heme copper oxidase complex ion transport membrane proteins Membrane Proteins - chemistry Membrane Proteins - genetics Microbiology Molecular Sequence Data Mutation - genetics nitrogen fixation Operon - genetics Oxygen - pharmacology Rhizobiaceae - enzymology Rhizobiaceae - genetics Sequence Alignment Sequence Analysis structural genes structure-activity relationships symbiosis transcription (genetics) Transcription, Genetic |
title | Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb3-type cytochrome oxidase |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T18%3A14%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Bradyrhizobium%20japonicum%20fixGHIS%20genes%20are%20required%20for%20the%20formation%20of%20the%20high-affinity%20cbb3-type%20cytochrome%20oxidase&rft.jtitle=Archives%20of%20microbiology&rft.au=Preisig,%20O&rft.date=1996-05&rft.volume=165&rft.issue=5&rft.spage=297&rft.epage=305&rft.pages=297-305&rft.issn=0302-8933&rft.eissn=1432-072X&rft.coden=AMICCW&rft_id=info:doi/10.1007/s002030050330&rft_dat=%3Cproquest_pubme%3E78069913%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=78069913&rft_id=info:pmid/8661920&rfr_iscdi=true |