2.50
Hdl Handle:
http://hdl.handle.net/10033/48541
Title:
Proteomic insights into metabolic adaptations in Alcanivorax borkumensis induced by alkane utilization.
Authors:
Sabirova, Julia S ( 0000-0002-7381-4748 ) ; Ferrer, Manuel; Regenhardt, Daniela; Timmis, Kenneth N; Golyshin, Peter N
Abstract:
Alcanivorax borkumensis is a ubiquitous marine petroleum oil-degrading bacterium with an unusual physiology specialized for alkane metabolism. This "hydrocarbonoclastic" bacterium degrades an exceptionally broad range of alkane hydrocarbons but few other substrates. The proteomic analysis presented here reveals metabolic features of the hydrocarbonoclastic lifestyle. Specifically, hexadecane-grown and pyruvate-grown cells differed in the expression of 97 cytoplasmic and membrane-associated proteins whose genes appeared to be components of 46 putative operon structures. Membrane proteins up-regulated in alkane-grown cells included three enzyme systems able to convert alkanes via terminal oxidation to fatty acids, namely, enzymes encoded by the well-known alkB1 gene cluster and two new alkane hydroxylating systems, a P450 cytochrome monooxygenase and a putative flavin-binding monooxygenase, and enzymes mediating beta-oxidation of fatty acids. Cytoplasmic proteins up-regulated in hexadecane-grown cells reflect a central metabolism based on a fatty acid diet, namely, enzymes of the glyoxylate bypass and of the gluconeogenesis pathway, able to provide key metabolic intermediates, like phosphoenolpyruvate, from fatty acids. They also include enzymes for synthesis of riboflavin and of unsaturated fatty acids and cardiolipin, which presumably reflect membrane restructuring required for membranes to adapt to perturbations induced by the massive influx of alkane oxidation enzymes. Ancillary functions up-regulated included the lipoprotein releasing system (Lol), presumably associated with biosurfactant release, and polyhydroxyalkanoate synthesis enzymes associated with carbon storage under conditions of carbon surfeit. The existence of three different alkane-oxidizing systems is consistent with the broad range of oil hydrocarbons degraded by A. borkumensis and its ecological success in oil-contaminated marine habitats.
Affiliation:
Institute of Microbiology, Technical University of Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany. jsa05@gbf.de
Citation:
Proteomic insights into metabolic adaptations in Alcanivorax borkumensis induced by alkane utilization. 2006, 188 (11):3763-73 J. Bacteriol.
Journal:
Journal of bacteriology
Issue Date:
Jun-2006
URI:
http://hdl.handle.net/10033/48541
DOI:
10.1128/JB.00072-06
PubMed ID:
16707669
Type:
Article
Language:
en
ISSN:
0021-9193
Appears in Collections:
Publications of RG Environmental Microbiology (UMW)

Full metadata record

DC FieldValue Language
dc.contributor.authorSabirova, Julia S-
dc.contributor.authorFerrer, Manuel-
dc.contributor.authorRegenhardt, Daniela-
dc.contributor.authorTimmis, Kenneth N-
dc.contributor.authorGolyshin, Peter N-
dc.date.accessioned2009-02-05T14:47:27Z-
dc.date.available2009-02-05T14:47:27Z-
dc.date.issued2006-06-
dc.identifier.citationProteomic insights into metabolic adaptations in Alcanivorax borkumensis induced by alkane utilization. 2006, 188 (11):3763-73 J. Bacteriol.en
dc.identifier.issn0021-9193-
dc.identifier.pmid16707669-
dc.identifier.doi10.1128/JB.00072-06-
dc.identifier.urihttp://hdl.handle.net/10033/48541-
dc.description.abstractAlcanivorax borkumensis is a ubiquitous marine petroleum oil-degrading bacterium with an unusual physiology specialized for alkane metabolism. This "hydrocarbonoclastic" bacterium degrades an exceptionally broad range of alkane hydrocarbons but few other substrates. The proteomic analysis presented here reveals metabolic features of the hydrocarbonoclastic lifestyle. Specifically, hexadecane-grown and pyruvate-grown cells differed in the expression of 97 cytoplasmic and membrane-associated proteins whose genes appeared to be components of 46 putative operon structures. Membrane proteins up-regulated in alkane-grown cells included three enzyme systems able to convert alkanes via terminal oxidation to fatty acids, namely, enzymes encoded by the well-known alkB1 gene cluster and two new alkane hydroxylating systems, a P450 cytochrome monooxygenase and a putative flavin-binding monooxygenase, and enzymes mediating beta-oxidation of fatty acids. Cytoplasmic proteins up-regulated in hexadecane-grown cells reflect a central metabolism based on a fatty acid diet, namely, enzymes of the glyoxylate bypass and of the gluconeogenesis pathway, able to provide key metabolic intermediates, like phosphoenolpyruvate, from fatty acids. They also include enzymes for synthesis of riboflavin and of unsaturated fatty acids and cardiolipin, which presumably reflect membrane restructuring required for membranes to adapt to perturbations induced by the massive influx of alkane oxidation enzymes. Ancillary functions up-regulated included the lipoprotein releasing system (Lol), presumably associated with biosurfactant release, and polyhydroxyalkanoate synthesis enzymes associated with carbon storage under conditions of carbon surfeit. The existence of three different alkane-oxidizing systems is consistent with the broad range of oil hydrocarbons degraded by A. borkumensis and its ecological success in oil-contaminated marine habitats.en
dc.language.isoenen
dc.subject.meshAdaptation, Physiologicalen
dc.subject.meshAlkanesen
dc.subject.meshBacterial Proteinsen
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen
dc.subject.meshEnzymesen
dc.subject.meshGenome, Bacterialen
dc.subject.meshHalomonadaceaeen
dc.subject.meshProteomeen
dc.subject.meshPyruvatesen
dc.titleProteomic insights into metabolic adaptations in Alcanivorax borkumensis induced by alkane utilization.en
dc.typeArticleen
dc.contributor.departmentInstitute of Microbiology, Technical University of Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany. jsa05@gbf.deen
dc.identifier.journalJournal of bacteriologyen

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