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Article: Multiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5
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TitleMultiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5
 
AuthorsLiu, C3 2 1
Wang, W2 3
Wu, Y2 3
Zhou, Z2 3
Lai, Q3
Shao, Z3
 
Issue Date2011
 
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EMI
 
CitationEnvironmental Microbiology, 2011, v. 13 n. 5, p. 1168-1178 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1462-2920.2010.02416.x
 
AbstractAlcanivorax dieselolei strain B-5 is a marine bacterium that can utilize a broad range of n-alkanes (C 5-C 36) as sole carbon source. However, the mechanisms responsible for this trait remain to be established. Here we report on the characterization of four alkane hydroxylases from A. dieselolei, including two homologues of AlkB (AlkB1 and AlkB2), a CYP153 homologue (P450), as well as an AlmA-like (AlmA) alkane hydroxylase. Heterologous expression of alkB1, alkB2, p450 and almA in Pseudomonas putida GPo12 (pGEc47ΔB) or P. fluorescens KOB2Δ1 verified their functions in alkane oxidation. Quantitative real-time RT-PCR analysis showed that these genes could be induced by alkanes ranging from C 8 to C 36. Notably, the expression of the p450 and almA genes was only upregulated in the presence of medium-chain (C 8-C 16) or long-chain (C 22-C 36) n-alkanes, respectively; while alkB1 and alkB2 responded to both medium- and long-chain n-alkanes (C 12-C 26). Moreover, branched alkanes (pristane and phytane) significantly elevated alkB1 and almA expression levels. Our findings demonstrate that the multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range. © 2011 Society for Applied Microbiology and Blackwell Publishing Ltd.
 
ISSN1462-2912
2013 Impact Factor: 6.240
 
DOIhttp://dx.doi.org/10.1111/j.1462-2920.2010.02416.x
 
ISI Accession Number IDWOS:000289798600005
 
DC FieldValue
dc.contributor.authorLiu, C
 
dc.contributor.authorWang, W
 
dc.contributor.authorWu, Y
 
dc.contributor.authorZhou, Z
 
dc.contributor.authorLai, Q
 
dc.contributor.authorShao, Z
 
dc.date.accessioned2012-09-20T07:51:44Z
 
dc.date.available2012-09-20T07:51:44Z
 
dc.date.issued2011
 
dc.description.abstractAlcanivorax dieselolei strain B-5 is a marine bacterium that can utilize a broad range of n-alkanes (C 5-C 36) as sole carbon source. However, the mechanisms responsible for this trait remain to be established. Here we report on the characterization of four alkane hydroxylases from A. dieselolei, including two homologues of AlkB (AlkB1 and AlkB2), a CYP153 homologue (P450), as well as an AlmA-like (AlmA) alkane hydroxylase. Heterologous expression of alkB1, alkB2, p450 and almA in Pseudomonas putida GPo12 (pGEc47ΔB) or P. fluorescens KOB2Δ1 verified their functions in alkane oxidation. Quantitative real-time RT-PCR analysis showed that these genes could be induced by alkanes ranging from C 8 to C 36. Notably, the expression of the p450 and almA genes was only upregulated in the presence of medium-chain (C 8-C 16) or long-chain (C 22-C 36) n-alkanes, respectively; while alkB1 and alkB2 responded to both medium- and long-chain n-alkanes (C 12-C 26). Moreover, branched alkanes (pristane and phytane) significantly elevated alkB1 and almA expression levels. Our findings demonstrate that the multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range. © 2011 Society for Applied Microbiology and Blackwell Publishing Ltd.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationEnvironmental Microbiology, 2011, v. 13 n. 5, p. 1168-1178 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1462-2920.2010.02416.x
 
dc.identifier.doihttp://dx.doi.org/10.1111/j.1462-2920.2010.02416.x
 
dc.identifier.epage1178
 
dc.identifier.hkuros209387
 
dc.identifier.isiWOS:000289798600005
 
dc.identifier.issn1462-2912
2013 Impact Factor: 6.240
 
dc.identifier.issue5
 
dc.identifier.openurl
 
dc.identifier.pmid21261799
 
dc.identifier.scopuseid_2-s2.0-79955013063
 
dc.identifier.spage1168
 
dc.identifier.urihttp://hdl.handle.net/10722/163794
 
dc.identifier.volume13
 
dc.languageeng
 
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EMI
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofEnvironmental Microbiology
 
dc.rightsThe definitive version is available at www.blackwell-synergy.com
 
dc.subject.meshAlcanivoraceae - enzymology - genetics
 
dc.subject.meshAlkane 1-Monooxygenase - genetics - metabolism
 
dc.subject.meshAlkanes - metabolism
 
dc.subject.meshCloning, Molecular
 
dc.subject.meshCytochrome P-450 Enzyme System - genetics - metabolism
 
dc.titleMultiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5
 
dc.typeArticle
 
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<contributor.author>Lai, Q</contributor.author>
<contributor.author>Shao, Z</contributor.author>
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<description.abstract>Alcanivorax dieselolei strain B-5 is a marine bacterium that can utilize a broad range of n-alkanes (C 5-C 36) as sole carbon source. However, the mechanisms responsible for this trait remain to be established. Here we report on the characterization of four alkane hydroxylases from A. dieselolei, including two homologues of AlkB (AlkB1 and AlkB2), a CYP153 homologue (P450), as well as an AlmA-like (AlmA) alkane hydroxylase. Heterologous expression of alkB1, alkB2, p450 and almA in Pseudomonas putida GPo12 (pGEc47&#916;B) or P. fluorescens KOB2&#916;1 verified their functions in alkane oxidation. Quantitative real-time RT-PCR analysis showed that these genes could be induced by alkanes ranging from C 8 to C 36. Notably, the expression of the p450 and almA genes was only upregulated in the presence of medium-chain (C 8-C 16) or long-chain (C 22-C 36) n-alkanes, respectively; while alkB1 and alkB2 responded to both medium- and long-chain n-alkanes (C 12-C 26). Moreover, branched alkanes (pristane and phytane) significantly elevated alkB1 and almA expression levels. Our findings demonstrate that the multiple alkane hydroxylase systems ensure the utilization of substrates of a broad chain length range. &#169; 2011 Society for Applied Microbiology and Blackwell Publishing Ltd.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. Xiamen University
  3. State Oceanic Administration China