MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?
Mercury resistance determinants are widespread in Gram-negative bacteria, but vary in the number and identity of genes present. We have shown that the merF gene from plasmid pMER327/419 encodes a 8.7 kDa mercury transport protein, by determining in vivo mercury volatilisation when MerF is expressed...
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| Veröffentlicht in: | FEBS letters 2000-04, Vol.472 (1), p.78-82 |
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| creator | Wilson, Jon R. Leang, Ching Morby, Andrew P. Hobman, Jon L. Brown, Nigel L. |
| description | Mercury resistance determinants are widespread in Gram-negative bacteria, but vary in the number and identity of genes present. We have shown that the
merF gene from plasmid pMER327/419 encodes a 8.7 kDa mercury transport protein, by determining in vivo mercury volatilisation when MerF is expressed in the presence of mercuric reductase. We have confirmed that MerC of Tn
21 is also a mercuric ion transporter. We have been able to detect interaction of the periplasmic protein MerP only with the MerT transporter, and not with MerF or MerC. Hydropathy analysis led to the prediction of models for MerT, MerC and MerF having three, four and two transmembrane regions respectively. In all three cases one pair of cysteine residues is predicted to be within the inner membrane with a second pair of cysteine residues on the cytoplasmic face, and the second helix contains a proline and at least one charged residue. The mechanisms of mercuric ion transport may be similar in these transporters even though their structures in the membrane differ. |
| doi_str_mv | 10.1016/S0014-5793(00)01430-7 |
| format | Article |
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merF gene from plasmid pMER327/419 encodes a 8.7 kDa mercury transport protein, by determining in vivo mercury volatilisation when MerF is expressed in the presence of mercuric reductase. We have confirmed that MerC of Tn
21 is also a mercuric ion transporter. We have been able to detect interaction of the periplasmic protein MerP only with the MerT transporter, and not with MerF or MerC. Hydropathy analysis led to the prediction of models for MerT, MerC and MerF having three, four and two transmembrane regions respectively. In all three cases one pair of cysteine residues is predicted to be within the inner membrane with a second pair of cysteine residues on the cytoplasmic face, and the second helix contains a proline and at least one charged residue. The mechanisms of mercuric ion transport may be similar in these transporters even though their structures in the membrane differ.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(00)01430-7</identifier><identifier>PMID: 10781809</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Bacterial Proteins ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Cation Transport Proteins ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - chemistry ; Escherichia coli - metabolism ; Integral membrane protein ; Ion Transport ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; MerC ; Mercury - metabolism ; Mercury resistance ; MerF ; MerT ; Models, Biological ; Molecular Sequence Data ; Plasmids ; Protein structure</subject><ispartof>FEBS letters, 2000-04, Vol.472 (1), p.78-82</ispartof><rights>2000 Federation of European Biochemical Societies</rights><rights>FEBS Letters 472 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5447-dff4d18489c2df2448c38b2f907db7bbaa3b8f4c30a32c454b81fe144b456a1a3</citedby><cites>FETCH-LOGICAL-c5447-dff4d18489c2df2448c38b2f907db7bbaa3b8f4c30a32c454b81fe144b456a1a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2800%2901430-7$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(00)01430-7$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,1414,1430,3539,27911,27912,45561,45562,45982,46396,46820</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10781809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilson, Jon R.</creatorcontrib><creatorcontrib>Leang, Ching</creatorcontrib><creatorcontrib>Morby, Andrew P.</creatorcontrib><creatorcontrib>Hobman, Jon L.</creatorcontrib><creatorcontrib>Brown, Nigel L.</creatorcontrib><title>MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Mercury resistance determinants are widespread in Gram-negative bacteria, but vary in the number and identity of genes present. We have shown that the
merF gene from plasmid pMER327/419 encodes a 8.7 kDa mercury transport protein, by determining in vivo mercury volatilisation when MerF is expressed in the presence of mercuric reductase. We have confirmed that MerC of Tn
21 is also a mercuric ion transporter. We have been able to detect interaction of the periplasmic protein MerP only with the MerT transporter, and not with MerF or MerC. Hydropathy analysis led to the prediction of models for MerT, MerC and MerF having three, four and two transmembrane regions respectively. In all three cases one pair of cysteine residues is predicted to be within the inner membrane with a second pair of cysteine residues on the cytoplasmic face, and the second helix contains a proline and at least one charged residue. The mechanisms of mercuric ion transport may be similar in these transporters even though their structures in the membrane differ.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Cation Transport Proteins</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli - metabolism</subject><subject>Integral membrane protein</subject><subject>Ion Transport</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>MerC</subject><subject>Mercury - metabolism</subject><subject>Mercury resistance</subject><subject>MerF</subject><subject>MerT</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Plasmids</subject><subject>Protein structure</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u3CAUhVHUKJn8PEIqVlW6cAoGD7ibKIkySaVUXaRdI8AXlWhspoBbzdsXj0dRdu0KuPecc-EDoQtKriihy0_PhFBeNaJll4R8LHtGKnGAFlQKVjG-lO_Q4lVyjE5SeiHlLGl7hI4pEZJK0i5Q-ApxhX3CGvcQ7Ri3OEc9pE2IGW9iyOCHz7jzzkGEIeOU42jzGCFhM-bisqHvw1DM9qcefOqxC3Ef5S32pfWaBzFdn6FDp9cJzvfrKfqxuv9-91g9fXv4cnfzVNmGc1F1zvGOSi5bW3eu5lxaJk3tWiI6I4zRmhnpuGVEs9ryhhtJHVDODW-Wmmp2ij7MueUNv0ZIWfU-WViv9QBhTErQiYGgRdjMQhtDShGc2kTf67hVlKiJtNqRVhNGRYjakVai-N7vB4ymh-6Na0ZbBI-z4I9fw_b_UtXq_rbedabG9F-lPM26nqOgEPvtIapkPQwWOh_BZtUF_4_b_gXCSqOG</recordid><startdate>20000421</startdate><enddate>20000421</enddate><creator>Wilson, Jon R.</creator><creator>Leang, Ching</creator><creator>Morby, Andrew P.</creator><creator>Hobman, Jon L.</creator><creator>Brown, Nigel L.</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>20000421</creationdate><title>MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?</title><author>Wilson, Jon R. ; Leang, Ching ; Morby, Andrew P. ; Hobman, Jon L. ; Brown, Nigel L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5447-dff4d18489c2df2448c38b2f907db7bbaa3b8f4c30a32c454b81fe144b456a1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Cation Transport Proteins</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - chemistry</topic><topic>Escherichia coli - metabolism</topic><topic>Integral membrane protein</topic><topic>Ion Transport</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>MerC</topic><topic>Mercury - metabolism</topic><topic>Mercury resistance</topic><topic>MerF</topic><topic>MerT</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>Plasmids</topic><topic>Protein structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilson, Jon R.</creatorcontrib><creatorcontrib>Leang, Ching</creatorcontrib><creatorcontrib>Morby, Andrew P.</creatorcontrib><creatorcontrib>Hobman, Jon L.</creatorcontrib><creatorcontrib>Brown, Nigel L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilson, Jon R.</au><au>Leang, Ching</au><au>Morby, Andrew P.</au><au>Hobman, Jon L.</au><au>Brown, Nigel L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2000-04-21</date><risdate>2000</risdate><volume>472</volume><issue>1</issue><spage>78</spage><epage>82</epage><pages>78-82</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Mercury resistance determinants are widespread in Gram-negative bacteria, but vary in the number and identity of genes present. We have shown that the
merF gene from plasmid pMER327/419 encodes a 8.7 kDa mercury transport protein, by determining in vivo mercury volatilisation when MerF is expressed in the presence of mercuric reductase. We have confirmed that MerC of Tn
21 is also a mercuric ion transporter. We have been able to detect interaction of the periplasmic protein MerP only with the MerT transporter, and not with MerF or MerC. Hydropathy analysis led to the prediction of models for MerT, MerC and MerF having three, four and two transmembrane regions respectively. In all three cases one pair of cysteine residues is predicted to be within the inner membrane with a second pair of cysteine residues on the cytoplasmic face, and the second helix contains a proline and at least one charged residue. The mechanisms of mercuric ion transport may be similar in these transporters even though their structures in the membrane differ.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10781809</pmid><doi>10.1016/S0014-5793(00)01430-7</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Bacterial Proteins Carrier Proteins - chemistry Carrier Proteins - metabolism Cation Transport Proteins Electrophoresis, Polyacrylamide Gel Escherichia coli - chemistry Escherichia coli - metabolism Integral membrane protein Ion Transport Membrane Proteins - chemistry Membrane Proteins - metabolism MerC Mercury - metabolism Mercury resistance MerF MerT Models, Biological Molecular Sequence Data Plasmids Protein structure |
| title | MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters? |
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