Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons
In this study, the enzymes involved in polycyclic aromatic hydrocarbon (PAH) degradation in the chrysene-degrading organism Sphingomonas sp. strain CHY-1 were investigated. [14C]chrysene mineralization experiments showed that PAH-grown bacteria produced high levels of chrysene-catabolic activity. On...
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description | In this study, the enzymes involved in polycyclic aromatic hydrocarbon (PAH) degradation in the chrysene-degrading organism Sphingomonas sp. strain CHY-1 were investigated. [14C]chrysene mineralization experiments showed that PAH-grown bacteria produced high levels of chrysene-catabolic activity. One PAH-induced protein displayed similarity with a ring-hydroxylating dioxygenase beta subunit, and a second PAH-induced protein displayed similarity with an extradiol dioxygenase. The genes encoding these proteins were cloned, and sequence analysis revealed two distinct loci containing clustered catabolic genes with strong similarities to corresponding genes found in Novosphingobium aromaticivorans F199. In the first locus, two genes potentially encoding a terminal dioxygenase component, designated PhnI, were followed by a gene coding for an aryl alcohol dehydrogenase (phnB). The second locus contained five genes encoding an extradiol dioxygenase (phnC), a ferredoxin (phnA3), another oxygenase component (PhnII), and an isomerase (phnD). PhnI was found to be capable of converting several PAHs, including chrysene, to the corresponding dihydrodiols. The activity of PhnI was greatly enhanced upon coexpression of genes encoding a ferredoxin (phnA3) and a reductase (phnA4). Disruption of the phnA1a gene encoding the PhnI alpha subunit resulted in a mutant strain that had lost the ability to grow on PAHs. The recombinant PhnII enzyme overproduced in Escherichia coli functioned as a salicylate 1-hydroxylase. PhnII also used methylsalicylates and anthranilate as substrates. Our results indicated that a single enzyme (PhnI) was responsible for the initial attack of a range of PAHs, including chrysene, in strain CHY-1. Furthermore, the conversion of salicylate to catechol was catalyzed by a three-component oxygenase unrelated to known salicylate hydroxylases. |
doi_str_mv | 10.1128/AEM.70.11.6714-6725.2004 |
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[14C]chrysene mineralization experiments showed that PAH-grown bacteria produced high levels of chrysene-catabolic activity. One PAH-induced protein displayed similarity with a ring-hydroxylating dioxygenase beta subunit, and a second PAH-induced protein displayed similarity with an extradiol dioxygenase. The genes encoding these proteins were cloned, and sequence analysis revealed two distinct loci containing clustered catabolic genes with strong similarities to corresponding genes found in Novosphingobium aromaticivorans F199. In the first locus, two genes potentially encoding a terminal dioxygenase component, designated PhnI, were followed by a gene coding for an aryl alcohol dehydrogenase (phnB). The second locus contained five genes encoding an extradiol dioxygenase (phnC), a ferredoxin (phnA3), another oxygenase component (PhnII), and an isomerase (phnD). PhnI was found to be capable of converting several PAHs, including chrysene, to the corresponding dihydrodiols. The activity of PhnI was greatly enhanced upon coexpression of genes encoding a ferredoxin (phnA3) and a reductase (phnA4). Disruption of the phnA1a gene encoding the PhnI alpha subunit resulted in a mutant strain that had lost the ability to grow on PAHs. The recombinant PhnII enzyme overproduced in Escherichia coli functioned as a salicylate 1-hydroxylase. PhnII also used methylsalicylates and anthranilate as substrates. Our results indicated that a single enzyme (PhnI) was responsible for the initial attack of a range of PAHs, including chrysene, in strain CHY-1. Furthermore, the conversion of salicylate to catechol was catalyzed by a three-component oxygenase unrelated to known salicylate hydroxylases.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/AEM.70.11.6714-6725.2004</identifier><identifier>PMID: 15528538</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; anthranilate ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biodegradation ; Biodegradation, Environmental ; Biological and medical sciences ; bioremediation ; chromosome mapping ; chrysene ; Chrysenes - metabolism ; Dioxygenases - chemistry ; Dioxygenases - genetics ; Dioxygenases - metabolism ; enzyme activity ; Enzymes ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; genes ; Hydrocarbons ; Microbiology ; mineralization ; Molecular Sequence Data ; Mutation ; Novosphingobium aromaticivorans ; nucleotide sequences ; oxygenases ; polycyclic aromatic hydrocarbons ; Polycyclic Aromatic Hydrocarbons - metabolism ; Sequence Analysis, DNA ; Sphingomonas ; Sphingomonas - enzymology ; Sphingomonas - genetics ; Sphingomonas - growth & development</subject><ispartof>Applied and Environmental Microbiology, 2004-11, Vol.70 (11), p.6714-6725</ispartof><rights>2005 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Nov 2004</rights><rights>Copyright © 2004, American Society for Microbiology 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c622t-454b11d2a03861e5d5730aba5e94ae1671b094dc7d4d6cd619f7bc76e01aa0ad3</citedby><cites>FETCH-LOGICAL-c622t-454b11d2a03861e5d5730aba5e94ae1671b094dc7d4d6cd619f7bc76e01aa0ad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC525238/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC525238/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,3188,3189,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16264497$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15528538$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Demaneche, S</creatorcontrib><creatorcontrib>Meyer, C</creatorcontrib><creatorcontrib>Micoud, J</creatorcontrib><creatorcontrib>Louwagie, M</creatorcontrib><creatorcontrib>Willison, J.C</creatorcontrib><creatorcontrib>Jouanneau, Y</creatorcontrib><title>Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>In this study, the enzymes involved in polycyclic aromatic hydrocarbon (PAH) degradation in the chrysene-degrading organism Sphingomonas sp. strain CHY-1 were investigated. [14C]chrysene mineralization experiments showed that PAH-grown bacteria produced high levels of chrysene-catabolic activity. One PAH-induced protein displayed similarity with a ring-hydroxylating dioxygenase beta subunit, and a second PAH-induced protein displayed similarity with an extradiol dioxygenase. The genes encoding these proteins were cloned, and sequence analysis revealed two distinct loci containing clustered catabolic genes with strong similarities to corresponding genes found in Novosphingobium aromaticivorans F199. In the first locus, two genes potentially encoding a terminal dioxygenase component, designated PhnI, were followed by a gene coding for an aryl alcohol dehydrogenase (phnB). The second locus contained five genes encoding an extradiol dioxygenase (phnC), a ferredoxin (phnA3), another oxygenase component (PhnII), and an isomerase (phnD). PhnI was found to be capable of converting several PAHs, including chrysene, to the corresponding dihydrodiols. The activity of PhnI was greatly enhanced upon coexpression of genes encoding a ferredoxin (phnA3) and a reductase (phnA4). Disruption of the phnA1a gene encoding the PhnI alpha subunit resulted in a mutant strain that had lost the ability to grow on PAHs. The recombinant PhnII enzyme overproduced in Escherichia coli functioned as a salicylate 1-hydroxylase. PhnII also used methylsalicylates and anthranilate as substrates. Our results indicated that a single enzyme (PhnI) was responsible for the initial attack of a range of PAHs, including chrysene, in strain CHY-1. Furthermore, the conversion of salicylate to catechol was catalyzed by a three-component oxygenase unrelated to known salicylate hydroxylases.</description><subject>Amino Acid Sequence</subject><subject>anthranilate</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biodegradation</subject><subject>Biodegradation, Environmental</subject><subject>Biological and medical sciences</subject><subject>bioremediation</subject><subject>chromosome mapping</subject><subject>chrysene</subject><subject>Chrysenes - metabolism</subject><subject>Dioxygenases - chemistry</subject><subject>Dioxygenases - genetics</subject><subject>Dioxygenases - metabolism</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Hydrocarbons</subject><subject>Microbiology</subject><subject>mineralization</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Novosphingobium aromaticivorans</subject><subject>nucleotide sequences</subject><subject>oxygenases</subject><subject>polycyclic aromatic hydrocarbons</subject><subject>Polycyclic Aromatic Hydrocarbons - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>Sphingomonas</subject><subject>Sphingomonas - enzymology</subject><subject>Sphingomonas - genetics</subject><subject>Sphingomonas - growth & development</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkstu1DAUhiMEokPhFcBCgl0G2_ElWbCoqgKViliUrq0T28m4SuzBzrTkjXhMHGbUKWxY-djnO1f_RYEIXhNC6w9nF1_XcrHXQhJWCkn5mmLMnhQrgpu65FUlnhYrjJumpJThk-JFSrc4E1jUz4sTwjmteVWvil-XxvrJdU7D5IJH4A3qdl4vFxjyFYY5uYRCh6b7gCCGMYO6jM735WY2Mfych_zie2RctnvrIdmEugwiQNfbTXaFMSdLKE0RnEfTBiZkbB_BZPAOogu7hLZhmPWsB6cfiqA_-TXENvj0snjWwZDsq8N5Wtx8uvh-_qW8-vb58vzsqtSC0qlknLWEGAq4qgWx3HBZYWiB24aBJXldLW6Y0dIwI7QRpOlkq6WwmABgMNVp8XGfd7trR2t03k6EQW2jGyHOKoBTf3u826g-3ClOOa3qHP_-EB_Dj51Nkxpd0nYYwNs8pyJSClxL_H-QSdJQRjP49h_wNuxi_pikKOaNqBq-QPUe0jGkFG330DHBatGMyppRcrHVohm1aEYtmsmhrx9PfAw8iCQD7w4AJA1DF8Frl46coIKxRh4b3bh-c--iVZBGBXZ8VDdDb_ZQB0FBH3Oim2uKSZXFKmiTy_0G6_DlcQ</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>Demaneche, S</creator><creator>Meyer, C</creator><creator>Micoud, J</creator><creator>Louwagie, M</creator><creator>Willison, J.C</creator><creator>Jouanneau, Y</creator><general>American Society for Microbiology</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>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>5PM</scope></search><sort><creationdate>20041101</creationdate><title>Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons</title><author>Demaneche, S ; Meyer, C ; Micoud, J ; Louwagie, M ; Willison, J.C ; Jouanneau, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c622t-454b11d2a03861e5d5730aba5e94ae1671b094dc7d4d6cd619f7bc76e01aa0ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>anthranilate</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biodegradation</topic><topic>Biodegradation, Environmental</topic><topic>Biological and medical sciences</topic><topic>bioremediation</topic><topic>chromosome mapping</topic><topic>chrysene</topic><topic>Chrysenes - metabolism</topic><topic>Dioxygenases - chemistry</topic><topic>Dioxygenases - genetics</topic><topic>Dioxygenases - metabolism</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Hydrocarbons</topic><topic>Microbiology</topic><topic>mineralization</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Novosphingobium aromaticivorans</topic><topic>nucleotide sequences</topic><topic>oxygenases</topic><topic>polycyclic aromatic hydrocarbons</topic><topic>Polycyclic Aromatic Hydrocarbons - metabolism</topic><topic>Sequence Analysis, DNA</topic><topic>Sphingomonas</topic><topic>Sphingomonas - enzymology</topic><topic>Sphingomonas - genetics</topic><topic>Sphingomonas - growth & development</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Demaneche, S</creatorcontrib><creatorcontrib>Meyer, C</creatorcontrib><creatorcontrib>Micoud, J</creatorcontrib><creatorcontrib>Louwagie, M</creatorcontrib><creatorcontrib>Willison, J.C</creatorcontrib><creatorcontrib>Jouanneau, Y</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>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Demaneche, S</au><au>Meyer, C</au><au>Micoud, J</au><au>Louwagie, M</au><au>Willison, J.C</au><au>Jouanneau, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>70</volume><issue>11</issue><spage>6714</spage><epage>6725</epage><pages>6714-6725</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>In this study, the enzymes involved in polycyclic aromatic hydrocarbon (PAH) degradation in the chrysene-degrading organism Sphingomonas sp. strain CHY-1 were investigated. [14C]chrysene mineralization experiments showed that PAH-grown bacteria produced high levels of chrysene-catabolic activity. One PAH-induced protein displayed similarity with a ring-hydroxylating dioxygenase beta subunit, and a second PAH-induced protein displayed similarity with an extradiol dioxygenase. The genes encoding these proteins were cloned, and sequence analysis revealed two distinct loci containing clustered catabolic genes with strong similarities to corresponding genes found in Novosphingobium aromaticivorans F199. In the first locus, two genes potentially encoding a terminal dioxygenase component, designated PhnI, were followed by a gene coding for an aryl alcohol dehydrogenase (phnB). The second locus contained five genes encoding an extradiol dioxygenase (phnC), a ferredoxin (phnA3), another oxygenase component (PhnII), and an isomerase (phnD). PhnI was found to be capable of converting several PAHs, including chrysene, to the corresponding dihydrodiols. The activity of PhnI was greatly enhanced upon coexpression of genes encoding a ferredoxin (phnA3) and a reductase (phnA4). Disruption of the phnA1a gene encoding the PhnI alpha subunit resulted in a mutant strain that had lost the ability to grow on PAHs. The recombinant PhnII enzyme overproduced in Escherichia coli functioned as a salicylate 1-hydroxylase. PhnII also used methylsalicylates and anthranilate as substrates. Our results indicated that a single enzyme (PhnI) was responsible for the initial attack of a range of PAHs, including chrysene, in strain CHY-1. Furthermore, the conversion of salicylate to catechol was catalyzed by a three-component oxygenase unrelated to known salicylate hydroxylases.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>15528538</pmid><doi>10.1128/AEM.70.11.6714-6725.2004</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence anthranilate Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biodegradation Biodegradation, Environmental Biological and medical sciences bioremediation chromosome mapping chrysene Chrysenes - metabolism Dioxygenases - chemistry Dioxygenases - genetics Dioxygenases - metabolism enzyme activity Enzymes Escherichia coli Fundamental and applied biological sciences. Psychology genes Hydrocarbons Microbiology mineralization Molecular Sequence Data Mutation Novosphingobium aromaticivorans nucleotide sequences oxygenases polycyclic aromatic hydrocarbons Polycyclic Aromatic Hydrocarbons - metabolism Sequence Analysis, DNA Sphingomonas Sphingomonas - enzymology Sphingomonas - genetics Sphingomonas - growth & development |
title | Identification and functional analysis of two aromatic-ring-hydroxylating dioxygenases from a Sphingomonas strain that degrades various polycyclic aromatic hydrocarbons |
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