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An Iron-regulated Gene, magA, Encoding an Iron Transport Protein of Magnetospirillum sp. Strain AMB-1
Magnetospirillum sp. AMB-1 is a freshwater magnetic bacterium which synthesizes intracellular particles of magnetite (Fe O ). A genomic DNA fragment required for synthesis of magnetic particles was previously isolated from a nonmagnetic transposon Tn 5 mutant. We have determined the complete nucleot...
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Published in: | The Journal of biological chemistry 1995-11, Vol.270 (47), p.28392-28396 |
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creator | Nakamura, C Burgess, J G Sode, K Matsunaga, T |
description | Magnetospirillum sp. AMB-1 is a freshwater magnetic bacterium which synthesizes intracellular particles of magnetite (Fe O ). A genomic DNA fragment required for synthesis of magnetic particles was previously isolated from a nonmagnetic transposon
Tn 5 mutant. We have determined the complete nucleotide sequence of this fragment. The 2975-base pair region contains two putative
open reading frames. One open reading frame, designated magA , encodes a polypeptide which is homologous to the cation efflux proteins, the Escherichia coli potassium ion-translocating protein, KefC, and the putative Na /H -antiporter, NapA, from Enterococcus hirae . Northern hybridization demonstrated that the magA mRNA transcript is 1.3 kilobases in size, corresponding to the size of the magA gene. A functional promoter was located upstream from the magA gene, and the transcription in AMB-1 was regulated by environmental iron concentration. Vesicles isolated from E. coli in which the MagA protein was expressed exhibited iron accumulation ability. We consider that the MagA protein is an iron
transport involved in the synthesis of magnetic particles in AMB-1. |
doi_str_mv | 10.1074/jbc.270.47.28392 |
format | article |
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Tn 5 mutant. We have determined the complete nucleotide sequence of this fragment. The 2975-base pair region contains two putative
open reading frames. One open reading frame, designated magA , encodes a polypeptide which is homologous to the cation efflux proteins, the Escherichia coli potassium ion-translocating protein, KefC, and the putative Na /H -antiporter, NapA, from Enterococcus hirae . Northern hybridization demonstrated that the magA mRNA transcript is 1.3 kilobases in size, corresponding to the size of the magA gene. A functional promoter was located upstream from the magA gene, and the transcription in AMB-1 was regulated by environmental iron concentration. Vesicles isolated from E. coli in which the MagA protein was expressed exhibited iron accumulation ability. We consider that the MagA protein is an iron
transport involved in the synthesis of magnetic particles in AMB-1.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.47.28392</identifier><identifier>PMID: 7499342</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Bacteria - genetics ; Bacteria - isolation & purification ; Bacteria - metabolism ; Bacterial Proteins - chemistry ; Base Sequence ; Blotting, Northern ; Carrier Proteins - biosynthesis ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cation Transport Proteins ; Cloning, Molecular ; DNA Transposable Elements ; Enterococcus hirae ; Escherichia coli ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial - drug effects ; Iron - metabolism ; Iron - pharmacology ; Kinetics ; Magnetics ; Magnetospirillum ; Molecular Sequence Data ; Mutagenesis, Insertional ; Open Reading Frames ; Potassium Channels ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Restriction Mapping ; RNA, Messenger - analysis ; RNA, Messenger - biosynthesis ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of biological chemistry, 1995-11, Vol.270 (47), p.28392-28396</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-449cc745db923a3a2a78f85f18f6d4645b4cd29d9bdb7d4ff4c367201d4619743</citedby><cites>FETCH-LOGICAL-c462t-449cc745db923a3a2a78f85f18f6d4645b4cd29d9bdb7d4ff4c367201d4619743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7499342$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakamura, C</creatorcontrib><creatorcontrib>Burgess, J G</creatorcontrib><creatorcontrib>Sode, K</creatorcontrib><creatorcontrib>Matsunaga, T</creatorcontrib><title>An Iron-regulated Gene, magA, Encoding an Iron Transport Protein of Magnetospirillum sp. Strain AMB-1</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Magnetospirillum sp. AMB-1 is a freshwater magnetic bacterium which synthesizes intracellular particles of magnetite (Fe O ). A genomic DNA fragment required for synthesis of magnetic particles was previously isolated from a nonmagnetic transposon
Tn 5 mutant. We have determined the complete nucleotide sequence of this fragment. The 2975-base pair region contains two putative
open reading frames. One open reading frame, designated magA , encodes a polypeptide which is homologous to the cation efflux proteins, the Escherichia coli potassium ion-translocating protein, KefC, and the putative Na /H -antiporter, NapA, from Enterococcus hirae . Northern hybridization demonstrated that the magA mRNA transcript is 1.3 kilobases in size, corresponding to the size of the magA gene. A functional promoter was located upstream from the magA gene, and the transcription in AMB-1 was regulated by environmental iron concentration. Vesicles isolated from E. coli in which the MagA protein was expressed exhibited iron accumulation ability. We consider that the MagA protein is an iron
transport involved in the synthesis of magnetic particles in AMB-1.</description><subject>Amino Acid Sequence</subject><subject>Bacteria - genetics</subject><subject>Bacteria - isolation & purification</subject><subject>Bacteria - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cation Transport Proteins</subject><subject>Cloning, Molecular</subject><subject>DNA Transposable Elements</subject><subject>Enterococcus hirae</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins</subject><subject>Gene Expression Regulation, Bacterial - drug effects</subject><subject>Iron - metabolism</subject><subject>Iron - pharmacology</subject><subject>Kinetics</subject><subject>Magnetics</subject><subject>Magnetospirillum</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Insertional</subject><subject>Open Reading Frames</subject><subject>Potassium Channels</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - analysis</subject><subject>RNA, Messenger - biosynthesis</subject><subject>Sequence Homology, Amino Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNpVkEtLxDAUhYMoOj72boQsxNW0JmnaNMtx8AUjCiq4C2mSdiJtUpMW8d9bnUHwbu7iO-csPgBOMUoxYvTyvVIpYSilLCVlxskOmGFUZkmW47ddMEOI4ISTvDwAhzG-o-kox_tgn1HOM0pmwCwcvA_eJcE0YysHo-GtcWYOO9ks5vDaKa-ta6DcxOBLkC72PgzwKfjBWAd9DR9k48zgY2-Dbduxg7FP4fMQ5IQXD1cJPgZ7tWyjOdn-I_B6c_2yvEtWj7f3y8UqUbQgQ0IpV4rRXFecZDKTRLKyLvMal3WhaUHziipNuOaVrpimdU1VVjCC8AQxZzQ7Aheb3T74j9HEQXQ2KtO20hk_RoEZwiwviymINkEVfIzB1KIPtpPhS2AkfsyKyayYzArKxK_ZqXK23R6rzui_wlblxM83fG2b9acNRlTWq7Xp_s98A8WxfyA</recordid><startdate>19951124</startdate><enddate>19951124</enddate><creator>Nakamura, C</creator><creator>Burgess, J G</creator><creator>Sode, K</creator><creator>Matsunaga, T</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>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19951124</creationdate><title>An Iron-regulated Gene, magA, Encoding an Iron Transport Protein of Magnetospirillum sp. Strain AMB-1</title><author>Nakamura, C ; Burgess, J G ; Sode, K ; Matsunaga, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-449cc745db923a3a2a78f85f18f6d4645b4cd29d9bdb7d4ff4c367201d4619743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteria - genetics</topic><topic>Bacteria - isolation & purification</topic><topic>Bacteria - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cation Transport Proteins</topic><topic>Cloning, Molecular</topic><topic>DNA Transposable Elements</topic><topic>Enterococcus hirae</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins</topic><topic>Gene Expression Regulation, Bacterial - drug effects</topic><topic>Iron - metabolism</topic><topic>Iron - pharmacology</topic><topic>Kinetics</topic><topic>Magnetics</topic><topic>Magnetospirillum</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Insertional</topic><topic>Open Reading Frames</topic><topic>Potassium Channels</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - analysis</topic><topic>RNA, Messenger - biosynthesis</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakamura, C</creatorcontrib><creatorcontrib>Burgess, J G</creatorcontrib><creatorcontrib>Sode, K</creatorcontrib><creatorcontrib>Matsunaga, T</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakamura, C</au><au>Burgess, J G</au><au>Sode, K</au><au>Matsunaga, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An Iron-regulated Gene, magA, Encoding an Iron Transport Protein of Magnetospirillum sp. Strain AMB-1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-11-24</date><risdate>1995</risdate><volume>270</volume><issue>47</issue><spage>28392</spage><epage>28396</epage><pages>28392-28396</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Magnetospirillum sp. AMB-1 is a freshwater magnetic bacterium which synthesizes intracellular particles of magnetite (Fe O ). A genomic DNA fragment required for synthesis of magnetic particles was previously isolated from a nonmagnetic transposon
Tn 5 mutant. We have determined the complete nucleotide sequence of this fragment. The 2975-base pair region contains two putative
open reading frames. One open reading frame, designated magA , encodes a polypeptide which is homologous to the cation efflux proteins, the Escherichia coli potassium ion-translocating protein, KefC, and the putative Na /H -antiporter, NapA, from Enterococcus hirae . Northern hybridization demonstrated that the magA mRNA transcript is 1.3 kilobases in size, corresponding to the size of the magA gene. A functional promoter was located upstream from the magA gene, and the transcription in AMB-1 was regulated by environmental iron concentration. Vesicles isolated from E. coli in which the MagA protein was expressed exhibited iron accumulation ability. We consider that the MagA protein is an iron
transport involved in the synthesis of magnetic particles in AMB-1.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7499342</pmid><doi>10.1074/jbc.270.47.28392</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Bacteria - genetics Bacteria - isolation & purification Bacteria - metabolism Bacterial Proteins - chemistry Base Sequence Blotting, Northern Carrier Proteins - biosynthesis Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cation Transport Proteins Cloning, Molecular DNA Transposable Elements Enterococcus hirae Escherichia coli Escherichia coli Proteins Gene Expression Regulation, Bacterial - drug effects Iron - metabolism Iron - pharmacology Kinetics Magnetics Magnetospirillum Molecular Sequence Data Mutagenesis, Insertional Open Reading Frames Potassium Channels Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Restriction Mapping RNA, Messenger - analysis RNA, Messenger - biosynthesis Sequence Homology, Amino Acid |
title | An Iron-regulated Gene, magA, Encoding an Iron Transport Protein of Magnetospirillum sp. Strain AMB-1 |
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