Loading…
Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1
Novosphingobium pentaromativorans US6-1 is a halophilic marine bacterium able to degrade polycyclic aromatic hydrocarbons (PAHs). Genome sequence analysis revealed that the large plasmid pLA1 present in N. pentaromativorans US6-1 consists of 199 ORFs and possess putative biodegradation genes that ma...
Saved in:
Published in: | PloS one 2014-03, Vol.9 (6), p.e90812 |
---|---|
Main Authors: | , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43 |
---|---|
cites | cdi_FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43 |
container_end_page | |
container_issue | 6 |
container_start_page | e90812 |
container_title | PloS one |
container_volume | 9 |
creator | Yun, Sung Ho Choi, Chi-Won Lee, Sang-Yeop Lee, Yeol Gyun Kwon, Joseph Leem, Sun Hee Chung, Young Ho Kahng, Hyung-Yeel Kim, Sang Jin Kwon, Kae Kyoung Kim, Seung Il |
description | Novosphingobium pentaromativorans US6-1 is a halophilic marine bacterium able to degrade polycyclic aromatic hydrocarbons (PAHs). Genome sequence analysis revealed that the large plasmid pLA1 present in N. pentaromativorans US6-1 consists of 199 ORFs and possess putative biodegradation genes that may be involved in PAH degradation. 1-DE/LC-MS/MS analysis of N. pentaromativorans US6-1 cultured in the presence of different PAHs and monocyclic aromatic hydrocarbons (MAHs) identified approximately 1,000 and 1,400 proteins, respectively. Up-regulated biodegradation enzymes, including those belonging to pLA1, were quantitatively compared. Among the PAHs, phenanthrene induced the strongest up-regulation of extradiol cleavage pathway enzymes such as ring-hydroxylating dioxygenase, putative biphenyl-2,3-diol 1,2-dioxygenase, and catechol 2,3-dioxygenase in pLA1. These enzymes lead the initial step of the lower catabolic pathway of aromatic hydrocarbons through the extradiol cleavage pathway and participate in the attack of PAH ring cleavage, respectively. However, N. pentaromativorans US6-1 cultured with p-hydroxybenzoate induced activation of another extradiol cleavage pathway, the protocatechuate 4,5-dioxygenase pathway, that originated from chromosomal genes. These results suggest that N. pentaromativorans US6-1 utilizes two different extradiol pathways and plasmid pLA1 might play a key role in the biodegradation of PAH in N. pentaromativorans US6-1. |
doi_str_mv | 10.1371/journal.pone.0090812 |
format | article |
fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1504977652</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A478773305</galeid><doaj_id>oai_doaj_org_article_049a0d225c104fd18d151184ae6846c6</doaj_id><sourcerecordid>A478773305</sourcerecordid><originalsourceid>FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43</originalsourceid><addsrcrecordid>eNqNk29r1TAUxosobk6_gWhAEATvNWnTtH0jjOGfwXDinG_DaXJ6m9H21KR3eP04flKz3W7ugoLkRcPp73mSc3JOkjwVfCmyQry5oLUfoFuONOCS84qXIr2X7IsqSxcq5dn9O_u95FEIF5znWanUw2QvlYrHHd9Pfn32NCH1zjDTggczoXc_YXI0MGrY2EHonWXjyaFgDXlWO7K48mD_INRtzMZ00QE89TFuWLuxngz4mobA3MCmFlkP3g3I6u0R6_41-0SXFMbWDSuqY4CNOEyzxSV5iNLzM7UQj5MHDXQBn8zfg-T8_buvRx8XJ6cfjo8OTxamyMtpASU3CnOUJUrMVaqKurK1RY685BKhrhUWDW8qkXNZCQG2MJmtMpAlSIEyO0ieb33HjoKeyxv0NV4UKk8jcbwlLMGFHr2LOW00gdPXAfIrDT7m36GOGuA2TXMjuGysKK3IhSgloCqlMip6vZ1PW9c9WhNz99DtmO7-GVyrV3Sps0rGl6uiwYvZwNP3NYbpH1eeqRXEW7mhoWhmeheMPpRFWRRZFrviIFn-hYrLYuyM2GCNi_EdwasdQWQm_DGtYB2CPj778v_s6bdd9uUdtkXopjZQt75qtrALyi1oPIXgsbmtnOD6aj5uqqGv5kPP8xFlz-5W_VZ0MxDZbxHjDos</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1504977652</pqid></control><display><type>article</type><title>Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1</title><source>PubMed (Medline)</source><source>Publicly Available Content Database</source><creator>Yun, Sung Ho ; Choi, Chi-Won ; Lee, Sang-Yeop ; Lee, Yeol Gyun ; Kwon, Joseph ; Leem, Sun Hee ; Chung, Young Ho ; Kahng, Hyung-Yeel ; Kim, Sang Jin ; Kwon, Kae Kyoung ; Kim, Seung Il</creator><creatorcontrib>Yun, Sung Ho ; Choi, Chi-Won ; Lee, Sang-Yeop ; Lee, Yeol Gyun ; Kwon, Joseph ; Leem, Sun Hee ; Chung, Young Ho ; Kahng, Hyung-Yeel ; Kim, Sang Jin ; Kwon, Kae Kyoung ; Kim, Seung Il</creatorcontrib><description>Novosphingobium pentaromativorans US6-1 is a halophilic marine bacterium able to degrade polycyclic aromatic hydrocarbons (PAHs). Genome sequence analysis revealed that the large plasmid pLA1 present in N. pentaromativorans US6-1 consists of 199 ORFs and possess putative biodegradation genes that may be involved in PAH degradation. 1-DE/LC-MS/MS analysis of N. pentaromativorans US6-1 cultured in the presence of different PAHs and monocyclic aromatic hydrocarbons (MAHs) identified approximately 1,000 and 1,400 proteins, respectively. Up-regulated biodegradation enzymes, including those belonging to pLA1, were quantitatively compared. Among the PAHs, phenanthrene induced the strongest up-regulation of extradiol cleavage pathway enzymes such as ring-hydroxylating dioxygenase, putative biphenyl-2,3-diol 1,2-dioxygenase, and catechol 2,3-dioxygenase in pLA1. These enzymes lead the initial step of the lower catabolic pathway of aromatic hydrocarbons through the extradiol cleavage pathway and participate in the attack of PAH ring cleavage, respectively. However, N. pentaromativorans US6-1 cultured with p-hydroxybenzoate induced activation of another extradiol cleavage pathway, the protocatechuate 4,5-dioxygenase pathway, that originated from chromosomal genes. These results suggest that N. pentaromativorans US6-1 utilizes two different extradiol pathways and plasmid pLA1 might play a key role in the biodegradation of PAH in N. pentaromativorans US6-1.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0090812</identifier><identifier>PMID: 24608660</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Bacteria ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biodegradation ; Biodegradation, Environmental ; Biology ; Biphenyl ; Biphenyl (Compound) ; Biphenyl-2,3-diol 1,2-dioxygenase ; Catechin ; Catechol ; Catechol 2,3-dioxygenase ; Cleavage ; Cluster Analysis ; Comparative analysis ; Enzymes ; Gene Expression Regulation, Bacterial ; Genes ; Genomes ; Genomics ; Hydrocarbon-degrading bacteria ; Life sciences ; Mycobacterium ; Novosphingobium ; Novosphingobium pentaromativorans ; Nucleotide sequence ; Peptides ; Phenanthrene ; Plasmids ; Plasmids - genetics ; Polycyclic aromatic hydrocarbons ; Polycyclic Aromatic Hydrocarbons - metabolism ; Proteins ; Proteome - genetics ; Proteome - metabolism ; Proteomics ; Protocatechuate 4,5-dioxygenase ; Pseudomonas putida ; Sphingomonadaceae - genetics ; Sphingomonadaceae - metabolism ; Sphingomonas ; Streptococcus infections ; Transcriptional Activation</subject><ispartof>PloS one, 2014-03, Vol.9 (6), p.e90812</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Yun 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 Yun et al 2014 Yun et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43</citedby><cites>FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1504977652/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1504977652?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,44566,53766,53768,74869</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24608660$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yun, Sung Ho</creatorcontrib><creatorcontrib>Choi, Chi-Won</creatorcontrib><creatorcontrib>Lee, Sang-Yeop</creatorcontrib><creatorcontrib>Lee, Yeol Gyun</creatorcontrib><creatorcontrib>Kwon, Joseph</creatorcontrib><creatorcontrib>Leem, Sun Hee</creatorcontrib><creatorcontrib>Chung, Young Ho</creatorcontrib><creatorcontrib>Kahng, Hyung-Yeel</creatorcontrib><creatorcontrib>Kim, Sang Jin</creatorcontrib><creatorcontrib>Kwon, Kae Kyoung</creatorcontrib><creatorcontrib>Kim, Seung Il</creatorcontrib><title>Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Novosphingobium pentaromativorans US6-1 is a halophilic marine bacterium able to degrade polycyclic aromatic hydrocarbons (PAHs). Genome sequence analysis revealed that the large plasmid pLA1 present in N. pentaromativorans US6-1 consists of 199 ORFs and possess putative biodegradation genes that may be involved in PAH degradation. 1-DE/LC-MS/MS analysis of N. pentaromativorans US6-1 cultured in the presence of different PAHs and monocyclic aromatic hydrocarbons (MAHs) identified approximately 1,000 and 1,400 proteins, respectively. Up-regulated biodegradation enzymes, including those belonging to pLA1, were quantitatively compared. Among the PAHs, phenanthrene induced the strongest up-regulation of extradiol cleavage pathway enzymes such as ring-hydroxylating dioxygenase, putative biphenyl-2,3-diol 1,2-dioxygenase, and catechol 2,3-dioxygenase in pLA1. These enzymes lead the initial step of the lower catabolic pathway of aromatic hydrocarbons through the extradiol cleavage pathway and participate in the attack of PAH ring cleavage, respectively. However, N. pentaromativorans US6-1 cultured with p-hydroxybenzoate induced activation of another extradiol cleavage pathway, the protocatechuate 4,5-dioxygenase pathway, that originated from chromosomal genes. These results suggest that N. pentaromativorans US6-1 utilizes two different extradiol pathways and plasmid pLA1 might play a key role in the biodegradation of PAH in N. pentaromativorans US6-1.</description><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biodegradation</subject><subject>Biodegradation, Environmental</subject><subject>Biology</subject><subject>Biphenyl</subject><subject>Biphenyl (Compound)</subject><subject>Biphenyl-2,3-diol 1,2-dioxygenase</subject><subject>Catechin</subject><subject>Catechol</subject><subject>Catechol 2,3-dioxygenase</subject><subject>Cleavage</subject><subject>Cluster Analysis</subject><subject>Comparative analysis</subject><subject>Enzymes</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genes</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Hydrocarbon-degrading bacteria</subject><subject>Life sciences</subject><subject>Mycobacterium</subject><subject>Novosphingobium</subject><subject>Novosphingobium pentaromativorans</subject><subject>Nucleotide sequence</subject><subject>Peptides</subject><subject>Phenanthrene</subject><subject>Plasmids</subject><subject>Plasmids - genetics</subject><subject>Polycyclic aromatic hydrocarbons</subject><subject>Polycyclic Aromatic Hydrocarbons - metabolism</subject><subject>Proteins</subject><subject>Proteome - genetics</subject><subject>Proteome - metabolism</subject><subject>Proteomics</subject><subject>Protocatechuate 4,5-dioxygenase</subject><subject>Pseudomonas putida</subject><subject>Sphingomonadaceae - genetics</subject><subject>Sphingomonadaceae - metabolism</subject><subject>Sphingomonas</subject><subject>Streptococcus infections</subject><subject>Transcriptional Activation</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>eNqNk29r1TAUxosobk6_gWhAEATvNWnTtH0jjOGfwXDinG_DaXJ6m9H21KR3eP04flKz3W7ugoLkRcPp73mSc3JOkjwVfCmyQry5oLUfoFuONOCS84qXIr2X7IsqSxcq5dn9O_u95FEIF5znWanUw2QvlYrHHd9Pfn32NCH1zjDTggczoXc_YXI0MGrY2EHonWXjyaFgDXlWO7K48mD_INRtzMZ00QE89TFuWLuxngz4mobA3MCmFlkP3g3I6u0R6_41-0SXFMbWDSuqY4CNOEyzxSV5iNLzM7UQj5MHDXQBn8zfg-T8_buvRx8XJ6cfjo8OTxamyMtpASU3CnOUJUrMVaqKurK1RY685BKhrhUWDW8qkXNZCQG2MJmtMpAlSIEyO0ieb33HjoKeyxv0NV4UKk8jcbwlLMGFHr2LOW00gdPXAfIrDT7m36GOGuA2TXMjuGysKK3IhSgloCqlMip6vZ1PW9c9WhNz99DtmO7-GVyrV3Sps0rGl6uiwYvZwNP3NYbpH1eeqRXEW7mhoWhmeheMPpRFWRRZFrviIFn-hYrLYuyM2GCNi_EdwasdQWQm_DGtYB2CPj778v_s6bdd9uUdtkXopjZQt75qtrALyi1oPIXgsbmtnOD6aj5uqqGv5kPP8xFlz-5W_VZ0MxDZbxHjDos</recordid><startdate>20140307</startdate><enddate>20140307</enddate><creator>Yun, Sung Ho</creator><creator>Choi, Chi-Won</creator><creator>Lee, Sang-Yeop</creator><creator>Lee, Yeol Gyun</creator><creator>Kwon, Joseph</creator><creator>Leem, Sun Hee</creator><creator>Chung, Young Ho</creator><creator>Kahng, Hyung-Yeel</creator><creator>Kim, Sang Jin</creator><creator>Kwon, Kae Kyoung</creator><creator>Kim, Seung Il</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>IOV</scope><scope>ISR</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>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20140307</creationdate><title>Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1</title><author>Yun, Sung Ho ; Choi, Chi-Won ; Lee, Sang-Yeop ; Lee, Yeol Gyun ; Kwon, Joseph ; Leem, Sun Hee ; Chung, Young Ho ; Kahng, Hyung-Yeel ; Kim, Sang Jin ; Kwon, Kae Kyoung ; Kim, Seung Il</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Bacteria</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biodegradation</topic><topic>Biodegradation, Environmental</topic><topic>Biology</topic><topic>Biphenyl</topic><topic>Biphenyl (Compound)</topic><topic>Biphenyl-2,3-diol 1,2-dioxygenase</topic><topic>Catechin</topic><topic>Catechol</topic><topic>Catechol 2,3-dioxygenase</topic><topic>Cleavage</topic><topic>Cluster Analysis</topic><topic>Comparative analysis</topic><topic>Enzymes</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Genes</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Hydrocarbon-degrading bacteria</topic><topic>Life sciences</topic><topic>Mycobacterium</topic><topic>Novosphingobium</topic><topic>Novosphingobium pentaromativorans</topic><topic>Nucleotide sequence</topic><topic>Peptides</topic><topic>Phenanthrene</topic><topic>Plasmids</topic><topic>Plasmids - genetics</topic><topic>Polycyclic aromatic hydrocarbons</topic><topic>Polycyclic Aromatic Hydrocarbons - metabolism</topic><topic>Proteins</topic><topic>Proteome - genetics</topic><topic>Proteome - metabolism</topic><topic>Proteomics</topic><topic>Protocatechuate 4,5-dioxygenase</topic><topic>Pseudomonas putida</topic><topic>Sphingomonadaceae - genetics</topic><topic>Sphingomonadaceae - metabolism</topic><topic>Sphingomonas</topic><topic>Streptococcus infections</topic><topic>Transcriptional Activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yun, Sung Ho</creatorcontrib><creatorcontrib>Choi, Chi-Won</creatorcontrib><creatorcontrib>Lee, Sang-Yeop</creatorcontrib><creatorcontrib>Lee, Yeol Gyun</creatorcontrib><creatorcontrib>Kwon, Joseph</creatorcontrib><creatorcontrib>Leem, Sun Hee</creatorcontrib><creatorcontrib>Chung, Young Ho</creatorcontrib><creatorcontrib>Kahng, Hyung-Yeel</creatorcontrib><creatorcontrib>Kim, Sang Jin</creatorcontrib><creatorcontrib>Kwon, Kae Kyoung</creatorcontrib><creatorcontrib>Kim, Seung Il</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database (ProQuest)</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database (Proquest)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Database (Proquest)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>Biological Sciences</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>ProQuest Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest advanced technologies & aerospace journals</collection><collection>test</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</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>Yun, Sung Ho</au><au>Choi, Chi-Won</au><au>Lee, Sang-Yeop</au><au>Lee, Yeol Gyun</au><au>Kwon, Joseph</au><au>Leem, Sun Hee</au><au>Chung, Young Ho</au><au>Kahng, Hyung-Yeel</au><au>Kim, Sang Jin</au><au>Kwon, Kae Kyoung</au><au>Kim, Seung Il</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-03-07</date><risdate>2014</risdate><volume>9</volume><issue>6</issue><spage>e90812</spage><pages>e90812-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Novosphingobium pentaromativorans US6-1 is a halophilic marine bacterium able to degrade polycyclic aromatic hydrocarbons (PAHs). Genome sequence analysis revealed that the large plasmid pLA1 present in N. pentaromativorans US6-1 consists of 199 ORFs and possess putative biodegradation genes that may be involved in PAH degradation. 1-DE/LC-MS/MS analysis of N. pentaromativorans US6-1 cultured in the presence of different PAHs and monocyclic aromatic hydrocarbons (MAHs) identified approximately 1,000 and 1,400 proteins, respectively. Up-regulated biodegradation enzymes, including those belonging to pLA1, were quantitatively compared. Among the PAHs, phenanthrene induced the strongest up-regulation of extradiol cleavage pathway enzymes such as ring-hydroxylating dioxygenase, putative biphenyl-2,3-diol 1,2-dioxygenase, and catechol 2,3-dioxygenase in pLA1. These enzymes lead the initial step of the lower catabolic pathway of aromatic hydrocarbons through the extradiol cleavage pathway and participate in the attack of PAH ring cleavage, respectively. However, N. pentaromativorans US6-1 cultured with p-hydroxybenzoate induced activation of another extradiol cleavage pathway, the protocatechuate 4,5-dioxygenase pathway, that originated from chromosomal genes. These results suggest that N. pentaromativorans US6-1 utilizes two different extradiol pathways and plasmid pLA1 might play a key role in the biodegradation of PAH in N. pentaromativorans US6-1.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24608660</pmid><doi>10.1371/journal.pone.0090812</doi><tpages>e90812</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1932-6203 |
ispartof | PloS one, 2014-03, Vol.9 (6), p.e90812 |
issn | 1932-6203 1932-6203 |
language | eng |
recordid | cdi_plos_journals_1504977652 |
source | PubMed (Medline); Publicly Available Content Database |
subjects | Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Biodegradation Biodegradation, Environmental Biology Biphenyl Biphenyl (Compound) Biphenyl-2,3-diol 1,2-dioxygenase Catechin Catechol Catechol 2,3-dioxygenase Cleavage Cluster Analysis Comparative analysis Enzymes Gene Expression Regulation, Bacterial Genes Genomes Genomics Hydrocarbon-degrading bacteria Life sciences Mycobacterium Novosphingobium Novosphingobium pentaromativorans Nucleotide sequence Peptides Phenanthrene Plasmids Plasmids - genetics Polycyclic aromatic hydrocarbons Polycyclic Aromatic Hydrocarbons - metabolism Proteins Proteome - genetics Proteome - metabolism Proteomics Protocatechuate 4,5-dioxygenase Pseudomonas putida Sphingomonadaceae - genetics Sphingomonadaceae - metabolism Sphingomonas Streptococcus infections Transcriptional Activation |
title | Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1 |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T13%3A58%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Proteomic%20characterization%20of%20plasmid%20pLA1%20for%20biodegradation%20of%20polycyclic%20aromatic%20hydrocarbons%20in%20the%20marine%20bacterium,%20Novosphingobium%20pentaromativorans%20US6-1&rft.jtitle=PloS%20one&rft.au=Yun,%20Sung%20Ho&rft.date=2014-03-07&rft.volume=9&rft.issue=6&rft.spage=e90812&rft.pages=e90812-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0090812&rft_dat=%3Cgale_plos_%3EA478773305%3C/gale_plos_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c758t-a80c6e5e48e4e56267b9dbde0e0804eabb6e7f0f91504911ad7c3d93a48a41e43%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1504977652&rft_id=info:pmid/24608660&rft_galeid=A478773305&rfr_iscdi=true |