A Novel Cyanobacterial SmtB/ArsR Family Repressor Regulates the Expression of a CPx-ATPase and a Metallothionein in Response to Both Cu(I)/Ag(I) and Zn(II)/Cd(II)
A novel SmtB/ArsR family metalloregulator, denoted BxmR, has been identified and characterized from the cyanobacterium Oscillatoria brevis. Genetic and biochemical evidence reveals that BxmR represses the expression of both bxa1, encoding a CPx-ATPase metal transporter, as well as a divergently tran...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-04, Vol.279 (17), p.17810-17818 |
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| creator | Liu, Tong Nakashima, Susumu Hirose, Kazunobu Shibasaka, Mineo Katsuhara, Maki Ezaki, Bunichi Giedroc, David P. Kasamo, Kunihiro |
| description | A novel SmtB/ArsR family metalloregulator, denoted BxmR, has been identified and characterized from the cyanobacterium Oscillatoria brevis. Genetic and biochemical evidence reveals that BxmR represses the expression of both bxa1, encoding a CPx-ATPase metal transporter, as well as a divergently transcribed operon encoding bxmR and bmtA, a heavy metal sequestering metallothionein. Derepression of the expression of all three genes is mediated by both monovalent (Ag(I) and Cu(I)) and divalent (Zn(II) and Cd(II)) heavy metal ions, a novel property among SmtB/ArsR metal sensors. Electrophoretic gel mobility shift experiments reveal that apoBxmR forms multiple resolvable complexes with oligonucleotides containing a single 12-2-12 inverted repeat derived from one of the two operator/promoter regions with similar apparent affinities. Preincubation with either monovalent or divalent metal ions induces disassembly of both the BxmR-bxa1 and BxmR-bxmR/bmtA operator/promoter complexes. Interestingly, the temporal regulation of expression of bxa1 and bmtA mRNAs is different in O. brevis with bxa1 induced first upon heavy metal treatment, followed by bmtA/bxmR. A dynamic interplay among Bxa1, BmtA, and BxmR is proposed that maintains metal homeostasis in O. brevis by balancing the relative rates of metal storage and efflux of multiple heavy metal ions. |
| doi_str_mv | 10.1074/jbc.M310560200 |
| format | Article |
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Genetic and biochemical evidence reveals that BxmR represses the expression of both bxa1, encoding a CPx-ATPase metal transporter, as well as a divergently transcribed operon encoding bxmR and bmtA, a heavy metal sequestering metallothionein. Derepression of the expression of all three genes is mediated by both monovalent (Ag(I) and Cu(I)) and divalent (Zn(II) and Cd(II)) heavy metal ions, a novel property among SmtB/ArsR metal sensors. Electrophoretic gel mobility shift experiments reveal that apoBxmR forms multiple resolvable complexes with oligonucleotides containing a single 12-2-12 inverted repeat derived from one of the two operator/promoter regions with similar apparent affinities. Preincubation with either monovalent or divalent metal ions induces disassembly of both the BxmR-bxa1 and BxmR-bxmR/bmtA operator/promoter complexes. Interestingly, the temporal regulation of expression of bxa1 and bmtA mRNAs is different in O. brevis with bxa1 induced first upon heavy metal treatment, followed by bmtA/bxmR. A dynamic interplay among Bxa1, BmtA, and BxmR is proposed that maintains metal homeostasis in O. brevis by balancing the relative rates of metal storage and efflux of multiple heavy metal ions.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M310560200</identifier><identifier>PMID: 14960585</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphatases - chemistry ; Bacterial Proteins ; Base Sequence ; Binding Sites ; Biological Transport ; Blotting, Western ; Cadmium - chemistry ; Copper - chemistry ; Cyanobacteria - metabolism ; Cyanophyta ; DNA - chemistry ; DNA-Binding Proteins - metabolism ; Dose-Response Relationship, Drug ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Ions ; Metallothionein - metabolism ; Metals - metabolism ; Models, Genetic ; Molecular Sequence Data ; Oscillatoria brevis ; Promoter Regions, Genetic ; Protein Binding ; Protein Biosynthesis ; Recombinant Proteins - chemistry ; Repressor Proteins - chemistry ; Repressor Proteins - metabolism ; Repressor Proteins - physiology ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Silver - chemistry ; Time Factors ; Trans-Activators - metabolism ; Transcription, Genetic ; Zinc - chemistry ; Zinc - metabolism</subject><ispartof>The Journal of biological chemistry, 2004-04, Vol.279 (17), p.17810-17818</ispartof><rights>2004 © 2004 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c551t-45494bd60022a4a720b611647c1a640a251b4b976eb465657df843441114c3123</citedby><cites>FETCH-LOGICAL-c551t-45494bd60022a4a720b611647c1a640a251b4b976eb465657df843441114c3123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14960585$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Tong</creatorcontrib><creatorcontrib>Nakashima, Susumu</creatorcontrib><creatorcontrib>Hirose, Kazunobu</creatorcontrib><creatorcontrib>Shibasaka, Mineo</creatorcontrib><creatorcontrib>Katsuhara, Maki</creatorcontrib><creatorcontrib>Ezaki, Bunichi</creatorcontrib><creatorcontrib>Giedroc, David P.</creatorcontrib><creatorcontrib>Kasamo, Kunihiro</creatorcontrib><title>A Novel Cyanobacterial SmtB/ArsR Family Repressor Regulates the Expression of a CPx-ATPase and a Metallothionein in Response to Both Cu(I)/Ag(I) and Zn(II)/Cd(II)</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A novel SmtB/ArsR family metalloregulator, denoted BxmR, has been identified and characterized from the cyanobacterium Oscillatoria brevis. Genetic and biochemical evidence reveals that BxmR represses the expression of both bxa1, encoding a CPx-ATPase metal transporter, as well as a divergently transcribed operon encoding bxmR and bmtA, a heavy metal sequestering metallothionein. Derepression of the expression of all three genes is mediated by both monovalent (Ag(I) and Cu(I)) and divalent (Zn(II) and Cd(II)) heavy metal ions, a novel property among SmtB/ArsR metal sensors. Electrophoretic gel mobility shift experiments reveal that apoBxmR forms multiple resolvable complexes with oligonucleotides containing a single 12-2-12 inverted repeat derived from one of the two operator/promoter regions with similar apparent affinities. Preincubation with either monovalent or divalent metal ions induces disassembly of both the BxmR-bxa1 and BxmR-bxmR/bmtA operator/promoter complexes. Interestingly, the temporal regulation of expression of bxa1 and bmtA mRNAs is different in O. brevis with bxa1 induced first upon heavy metal treatment, followed by bmtA/bxmR. A dynamic interplay among Bxa1, BmtA, and BxmR is proposed that maintains metal homeostasis in O. brevis by balancing the relative rates of metal storage and efflux of multiple heavy metal ions.</description><subject>Adenosine Triphosphatases - chemistry</subject><subject>Bacterial Proteins</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological Transport</subject><subject>Blotting, Western</subject><subject>Cadmium - chemistry</subject><subject>Copper - chemistry</subject><subject>Cyanobacteria - metabolism</subject><subject>Cyanophyta</subject><subject>DNA - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Ions</subject><subject>Metallothionein - metabolism</subject><subject>Metals - metabolism</subject><subject>Models, Genetic</subject><subject>Molecular Sequence Data</subject><subject>Oscillatoria brevis</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Protein Biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - metabolism</subject><subject>Repressor Proteins - physiology</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Silver - chemistry</subject><subject>Time Factors</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription, Genetic</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</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>eNp1kU1v1DAQhi0EokvhyhH5gFA5ZNeT2Pk4plELK7VQLUVCXCzHmd24SuKtnZTu3-GX4u2u1BPWyGO9fmY09kvIe2BzYBlf3NV6fp0AEymLGXtBZsDyJEoE_HpJZozFEBWxyE_IG-_vWFi8gNfkBHiRMpGLGflb0m_2ATta7dRga6VHdEZ19Ec_ni9K51f0UvWm29EVbh16b104baZOjejp2CK9eHzSjR2oXVNFq5vHqLy9UR6pGpogXOOous6ObUDQDDTECv3WDoEYLT0PN7SazpafF-Um7E9Vv4ezZRCqZp_ekldr1Xl8d8yn5OflxW31Nbr6_mVZlVeRFgLGiAte8LpJw6NjxVUWszoFSHmmQaWcqVhAzesiS7HmqUhF1qxznnAOAFwnECen5NOh79bZ-wn9KHvjNXadGtBOXkLOhGBxFsD5AdTOeu9wLbfO9MrtJDC5d0UGV-SzK6Hgw7HzVPfYPONHGwLw8QC0ZtP-MQ5lbaxusZdxVkjIQuSw75MfMAzf8GDQSa8NDhqbUKJH2VjzvxH-AWVqoxw</recordid><startdate>20040423</startdate><enddate>20040423</enddate><creator>Liu, Tong</creator><creator>Nakashima, Susumu</creator><creator>Hirose, Kazunobu</creator><creator>Shibasaka, Mineo</creator><creator>Katsuhara, Maki</creator><creator>Ezaki, Bunichi</creator><creator>Giedroc, David P.</creator><creator>Kasamo, Kunihiro</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H97</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20040423</creationdate><title>A Novel Cyanobacterial SmtB/ArsR Family Repressor Regulates the Expression of a CPx-ATPase and a Metallothionein in Response to Both Cu(I)/Ag(I) and Zn(II)/Cd(II)</title><author>Liu, Tong ; 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Genetic and biochemical evidence reveals that BxmR represses the expression of both bxa1, encoding a CPx-ATPase metal transporter, as well as a divergently transcribed operon encoding bxmR and bmtA, a heavy metal sequestering metallothionein. Derepression of the expression of all three genes is mediated by both monovalent (Ag(I) and Cu(I)) and divalent (Zn(II) and Cd(II)) heavy metal ions, a novel property among SmtB/ArsR metal sensors. Electrophoretic gel mobility shift experiments reveal that apoBxmR forms multiple resolvable complexes with oligonucleotides containing a single 12-2-12 inverted repeat derived from one of the two operator/promoter regions with similar apparent affinities. Preincubation with either monovalent or divalent metal ions induces disassembly of both the BxmR-bxa1 and BxmR-bxmR/bmtA operator/promoter complexes. Interestingly, the temporal regulation of expression of bxa1 and bmtA mRNAs is different in O. brevis with bxa1 induced first upon heavy metal treatment, followed by bmtA/bxmR. A dynamic interplay among Bxa1, BmtA, and BxmR is proposed that maintains metal homeostasis in O. brevis by balancing the relative rates of metal storage and efflux of multiple heavy metal ions.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14960585</pmid><doi>10.1074/jbc.M310560200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2004-04, Vol.279 (17), p.17810-17818 |
| issn | 0021-9258 1083-351X |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - chemistry Bacterial Proteins Base Sequence Binding Sites Biological Transport Blotting, Western Cadmium - chemistry Copper - chemistry Cyanobacteria - metabolism Cyanophyta DNA - chemistry DNA-Binding Proteins - metabolism Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism Escherichia coli Proteins Ions Metallothionein - metabolism Metals - metabolism Models, Genetic Molecular Sequence Data Oscillatoria brevis Promoter Regions, Genetic Protein Binding Protein Biosynthesis Recombinant Proteins - chemistry Repressor Proteins - chemistry Repressor Proteins - metabolism Repressor Proteins - physiology Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - metabolism Sequence Homology, Amino Acid Silver - chemistry Time Factors Trans-Activators - metabolism Transcription, Genetic Zinc - chemistry Zinc - metabolism |
| title | A Novel Cyanobacterial SmtB/ArsR Family Repressor Regulates the Expression of a CPx-ATPase and a Metallothionein in Response to Both Cu(I)/Ag(I) and Zn(II)/Cd(II) |
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