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Nickel-resistance determinants in Acidiphilium sp. PM identified by genome-wide functional screening
Acidiphilium spp. are conspicuous dwellers of acidic, metal-rich environments. Indeed, they are among the most metal-resistant organisms; yet little is known about the mechanisms behind the metal tolerance in this genus. Acidiphilium sp. PM is an environmental isolate from Rio Tinto, an acidic, meta...
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Published in: | PloS one 2014-04, Vol.9 (4), p.e95041-e95041 |
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description | Acidiphilium spp. are conspicuous dwellers of acidic, metal-rich environments. Indeed, they are among the most metal-resistant organisms; yet little is known about the mechanisms behind the metal tolerance in this genus. Acidiphilium sp. PM is an environmental isolate from Rio Tinto, an acidic, metal-laden river located in southwestern Spain. The characterization of its metal resistance revealed a remarkable ability to tolerate high Ni concentrations. Here we report the screening of a genomic library of Acidiphilium sp. PM to identify genes involved in Ni resistance. This approach revealed seven different genes conferring Ni resistance to E. coli, two of which form an operon encoding the ATP-dependent protease HslVU (ClpQY). This protease was found to enhance resistance to both Ni and Co in E. coli, a function not previously reported. Other Ni-resistance determinants include genes involved in lipopolysaccharide biosynthesis and the synthesis of branched amino acids. The diversity of molecular functions of the genes recovered in the screening suggests that Ni resistance in Acidiphilium sp. PM probably relies on different molecular mechanisms. |
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PM identified by genome-wide functional screening</title><source>Publicly Available Content Database</source><source>PubMed Central</source><creator>San Martin-Uriz, Patxi ; Mirete, Salvador ; Alcolea, Pedro J ; Gomez, Manuel J ; Amils, Ricardo ; Gonzalez-Pastor, Jose E</creator><contributor>van Veen, Hendrik W.</contributor><creatorcontrib>San Martin-Uriz, Patxi ; Mirete, Salvador ; Alcolea, Pedro J ; Gomez, Manuel J ; Amils, Ricardo ; Gonzalez-Pastor, Jose E ; van Veen, Hendrik W.</creatorcontrib><description>Acidiphilium spp. are conspicuous dwellers of acidic, metal-rich environments. Indeed, they are among the most metal-resistant organisms; yet little is known about the mechanisms behind the metal tolerance in this genus. Acidiphilium sp. PM is an environmental isolate from Rio Tinto, an acidic, metal-laden river located in southwestern Spain. The characterization of its metal resistance revealed a remarkable ability to tolerate high Ni concentrations. Here we report the screening of a genomic library of Acidiphilium sp. PM to identify genes involved in Ni resistance. This approach revealed seven different genes conferring Ni resistance to E. coli, two of which form an operon encoding the ATP-dependent protease HslVU (ClpQY). This protease was found to enhance resistance to both Ni and Co in E. coli, a function not previously reported. Other Ni-resistance determinants include genes involved in lipopolysaccharide biosynthesis and the synthesis of branched amino acids. The diversity of molecular functions of the genes recovered in the screening suggests that Ni resistance in Acidiphilium sp. PM probably relies on different molecular mechanisms.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0095041</identifier><identifier>PMID: 24740277</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acidiphilium - genetics ; Acidiphilium - metabolism ; Amino acids ; Arsenic ; ATP-Dependent Proteases - genetics ; Bacteria - classification ; Bacteria - genetics ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biology and Life Sciences ; Biosynthesis ; Cell division ; Chemical synthesis ; Dehydrogenases ; Drug Resistance, Bacterial - genetics ; E coli ; Ecology and Environmental Sciences ; Enzymes ; Escherichia coli ; Gene expression ; Gene Transfer, Horizontal ; Genes ; Genome, Bacterial - genetics ; Genomes ; Genomic Library ; Lipopolysaccharides ; Lipopolysaccharides - biosynthesis ; Medical screening ; Metals ; Microbial Viability - drug effects ; Microbial Viability - genetics ; Microorganisms ; Molecular modelling ; Molecular Sequence Data ; Nickel ; Nickel - metabolism ; Nickel - pharmacology ; Open Reading Frames - genetics ; Operon ; Phylogeny ; Protease ; Proteinase ; Proteins ; Rivers ; Rivers - microbiology ; Sequence Analysis, DNA ; Spain</subject><ispartof>PloS one, 2014-04, Vol.9 (4), p.e95041-e95041</ispartof><rights>2014 San Martin-Uriz et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 San Martin-Uriz et al 2014 San Martin-Uriz et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c596t-4d27825d029e29128e64dc9e9d036a8d02bbc24ae1de95a191adfa2aae077f3f3</citedby><cites>FETCH-LOGICAL-c596t-4d27825d029e29128e64dc9e9d036a8d02bbc24ae1de95a191adfa2aae077f3f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1516953982/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1516953982?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25733,27903,27904,36991,36992,44569,53769,53771,74872</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24740277$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>van Veen, Hendrik W.</contributor><creatorcontrib>San Martin-Uriz, Patxi</creatorcontrib><creatorcontrib>Mirete, Salvador</creatorcontrib><creatorcontrib>Alcolea, Pedro J</creatorcontrib><creatorcontrib>Gomez, Manuel J</creatorcontrib><creatorcontrib>Amils, Ricardo</creatorcontrib><creatorcontrib>Gonzalez-Pastor, Jose E</creatorcontrib><title>Nickel-resistance determinants in Acidiphilium sp. PM identified by genome-wide functional screening</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Acidiphilium spp. are conspicuous dwellers of acidic, metal-rich environments. Indeed, they are among the most metal-resistant organisms; yet little is known about the mechanisms behind the metal tolerance in this genus. Acidiphilium sp. PM is an environmental isolate from Rio Tinto, an acidic, metal-laden river located in southwestern Spain. The characterization of its metal resistance revealed a remarkable ability to tolerate high Ni concentrations. Here we report the screening of a genomic library of Acidiphilium sp. PM to identify genes involved in Ni resistance. This approach revealed seven different genes conferring Ni resistance to E. coli, two of which form an operon encoding the ATP-dependent protease HslVU (ClpQY). This protease was found to enhance resistance to both Ni and Co in E. coli, a function not previously reported. Other Ni-resistance determinants include genes involved in lipopolysaccharide biosynthesis and the synthesis of branched amino acids. The diversity of molecular functions of the genes recovered in the screening suggests that Ni resistance in Acidiphilium sp. PM probably relies on different molecular mechanisms.</description><subject>Acidiphilium - genetics</subject><subject>Acidiphilium - metabolism</subject><subject>Amino acids</subject><subject>Arsenic</subject><subject>ATP-Dependent Proteases - genetics</subject><subject>Bacteria - classification</subject><subject>Bacteria - genetics</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biology and Life Sciences</subject><subject>Biosynthesis</subject><subject>Cell division</subject><subject>Chemical synthesis</subject><subject>Dehydrogenases</subject><subject>Drug Resistance, Bacterial - genetics</subject><subject>E coli</subject><subject>Ecology and Environmental Sciences</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Gene expression</subject><subject>Gene Transfer, Horizontal</subject><subject>Genes</subject><subject>Genome, Bacterial - genetics</subject><subject>Genomes</subject><subject>Genomic Library</subject><subject>Lipopolysaccharides</subject><subject>Lipopolysaccharides - biosynthesis</subject><subject>Medical screening</subject><subject>Metals</subject><subject>Microbial Viability - drug effects</subject><subject>Microbial Viability - genetics</subject><subject>Microorganisms</subject><subject>Molecular modelling</subject><subject>Molecular Sequence Data</subject><subject>Nickel</subject><subject>Nickel - metabolism</subject><subject>Nickel - pharmacology</subject><subject>Open Reading Frames - genetics</subject><subject>Operon</subject><subject>Phylogeny</subject><subject>Protease</subject><subject>Proteinase</subject><subject>Proteins</subject><subject>Rivers</subject><subject>Rivers - microbiology</subject><subject>Sequence Analysis, DNA</subject><subject>Spain</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptUstu1TAUjBAVLYU_QGCpGza5-BU73iBVFdBK5bGAteXYJ7e-JHawE1D_Hrc3rVrEytZ4ZjznaKrqFcEbwiR5t4tLCmbYTDHABmPVYE6eVEdEMVoLitnTB_fD6nnOO4wb1grxrDqkXHJMpTyq3Bdvf8JQJ8g-zyZYQA5mSKMPJswZ-YBOrXd-uvKDX0aUpw369hl5B2H2vQeHumu0hRBHqP8UFPVLsLOPJRnKNgEEH7YvqoPeDBlerudx9ePjh-9n5_Xl108XZ6eXtW2UmGvuqGxp4zBVQBWhLQjurALlMBOmLXjXWcoNEAeqMUQR43pDjQEsZc96dly92ftOQ8x6XVDWpCFCNUy1tDAu9gwXzU5PyY8mXetovL4FYtpqk2ZvB9CYYmicpYaB41JSRZkAYl1PTNs5QorX-_W3pRvB2bKRZIZHpo9fgr_S2_hblySKiqYYvF0NUvy1QJ716LOFYTAB4nKbW7Yt5pgX6sk_1P9Px_csm2LOCfr7MATrm9LcqfRNafRamiJ7_XCQe9FdS9hfq_HBwg</recordid><startdate>20140416</startdate><enddate>20140416</enddate><creator>San Martin-Uriz, Patxi</creator><creator>Mirete, Salvador</creator><creator>Alcolea, Pedro J</creator><creator>Gomez, Manuel J</creator><creator>Amils, Ricardo</creator><creator>Gonzalez-Pastor, Jose E</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20140416</creationdate><title>Nickel-resistance determinants in Acidiphilium sp. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>San Martin-Uriz, Patxi</au><au>Mirete, Salvador</au><au>Alcolea, Pedro J</au><au>Gomez, Manuel J</au><au>Amils, Ricardo</au><au>Gonzalez-Pastor, Jose E</au><au>van Veen, Hendrik W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nickel-resistance determinants in Acidiphilium sp. PM identified by genome-wide functional screening</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-04-16</date><risdate>2014</risdate><volume>9</volume><issue>4</issue><spage>e95041</spage><epage>e95041</epage><pages>e95041-e95041</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Acidiphilium spp. are conspicuous dwellers of acidic, metal-rich environments. Indeed, they are among the most metal-resistant organisms; yet little is known about the mechanisms behind the metal tolerance in this genus. Acidiphilium sp. PM is an environmental isolate from Rio Tinto, an acidic, metal-laden river located in southwestern Spain. The characterization of its metal resistance revealed a remarkable ability to tolerate high Ni concentrations. Here we report the screening of a genomic library of Acidiphilium sp. PM to identify genes involved in Ni resistance. This approach revealed seven different genes conferring Ni resistance to E. coli, two of which form an operon encoding the ATP-dependent protease HslVU (ClpQY). This protease was found to enhance resistance to both Ni and Co in E. coli, a function not previously reported. Other Ni-resistance determinants include genes involved in lipopolysaccharide biosynthesis and the synthesis of branched amino acids. The diversity of molecular functions of the genes recovered in the screening suggests that Ni resistance in Acidiphilium sp. PM probably relies on different molecular mechanisms.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24740277</pmid><doi>10.1371/journal.pone.0095041</doi><oa>free_for_read</oa></addata></record> |
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subjects | Acidiphilium - genetics Acidiphilium - metabolism Amino acids Arsenic ATP-Dependent Proteases - genetics Bacteria - classification Bacteria - genetics Bacterial Proteins - genetics Bacterial Proteins - metabolism Biology and Life Sciences Biosynthesis Cell division Chemical synthesis Dehydrogenases Drug Resistance, Bacterial - genetics E coli Ecology and Environmental Sciences Enzymes Escherichia coli Gene expression Gene Transfer, Horizontal Genes Genome, Bacterial - genetics Genomes Genomic Library Lipopolysaccharides Lipopolysaccharides - biosynthesis Medical screening Metals Microbial Viability - drug effects Microbial Viability - genetics Microorganisms Molecular modelling Molecular Sequence Data Nickel Nickel - metabolism Nickel - pharmacology Open Reading Frames - genetics Operon Phylogeny Protease Proteinase Proteins Rivers Rivers - microbiology Sequence Analysis, DNA Spain |
title | Nickel-resistance determinants in Acidiphilium sp. PM identified by genome-wide functional screening |
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