File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Multiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5

TitleMultiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5
Authors
Issue Date2011
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EMI
Citation
Environmental Microbiology, 2011, v. 13 n. 5, p. 1168-1178 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/163794
ISSN
2014 Impact Factor: 6.201
2014 SCImago Journal Rankings: 2.425
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiu, Cen_HK
dc.contributor.authorWang, Wen_HK
dc.contributor.authorWu, Yen_HK
dc.contributor.authorZhou, Zen_HK
dc.contributor.authorLai, Qen_HK
dc.contributor.authorShao, Zen_HK
dc.date.accessioned2012-09-20T07:51:44Z-
dc.date.available2012-09-20T07:51:44Z-
dc.date.issued2011en_HK
dc.identifier.citationEnvironmental Microbiology, 2011, v. 13 n. 5, p. 1168-1178en_HK
dc.identifier.issn1462-2912en_HK
dc.identifier.urihttp://hdl.handle.net/10722/163794-
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.en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EMIen_HK
dc.relation.ispartofEnvironmental Microbiologyen_HK
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-5en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1462-2920 (Electronic) 1462-2912 (Linkin&volume=13&issue=5&spage=1168&epage=78&date=2011&atitle=Multiple+alkane+hydroxylase+systems+in+a+marine+alkane+degrader,+Alcanivorax+dieselolei+B-5en_US
dc.identifier.emailLiu, C: lchenli@hku.hken_US
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1462-2920.2010.02416.xen_HK
dc.identifier.pmid21261799-
dc.identifier.scopuseid_2-s2.0-79955013063en_HK
dc.identifier.hkuros209387en_US
dc.identifier.volume13en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1168en_HK
dc.identifier.epage1178en_HK
dc.identifier.isiWOS:000289798600005-
dc.publisher.placeUnited Kingdomen_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats