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  • 1
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    Purification, Characterization, and Crystallization of the Components of the Nitrobenzene and 2-Nitrotoluene Dioxygenase Enzyme Systems
    American Society for Microbiology ; 2005
    In:  Applied and Environmental Microbiology Vol. 71, No. 7 ( 2005-07), p. 3806-3814
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 71, No. 7 ( 2005-07), p. 3806-3814
    Kurzfassung: The protein components of the 2-nitrotoluene (2NT) and nitrobenzene dioxygenase enzyme systems from Acidovorax sp. strain JS42 and Comamonas sp. strain JS765, respectively, were purified and characterized. These enzymes catalyze the initial step in the degradation of 2-nitrotoluene and nitrobenzene. The identical shared reductase and ferredoxin components were monomers of 35 and 11.5 kDa, respectively. The reductase component contained 1.86 g-atoms iron, 2.01 g-atoms sulfur, and one molecule of flavin adenine dinucleotide per monomer. Spectral properties of the reductase indicated the presence of a plant-type [2Fe-2S] center and a flavin. The reductase catalyzed the reduction of cytochrome c , ferricyanide, and 2,6-dichlorophenol indophenol. The ferredoxin contained 2.20 g-atoms iron and 1.99 g-atoms sulfur per monomer and had spectral properties indicative of a Rieske [2Fe-2S] center. The ferredoxin component could be effectively replaced by the ferredoxin from the Pseudomonas sp. strain NCIB 9816-4 naphthalene dioxygenase system but not by that from the Burkholderia sp. strain LB400 biphenyl or Pseudomonas putida F1 toluene dioxygenase system. The oxygenases from the 2-nitrotoluene and nitrobenzene dioxygenase systems each had spectral properties indicating the presence of a Rieske [2Fe-2S] center, and the subunit composition of each oxygenase was an α 3 β 3 hexamer. The apparent K m of 2-nitrotoluene dioxygenase for 2NT was 20 μM, and that for naphthalene was 121 μM. The specificity constants were 7.0 μM −1 min −1 for 2NT and 1.2 μM −1 min −1 for naphthalene, indicating that the enzyme is more efficient with 2NT as a substrate. Diffraction-quality crystals of the two oxygenases were obtained.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.71.7.3806-3814.2005
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2005
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
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  • 2
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    Purification, characterization, and crystallization of the components of a biphenyl dioxygenase system from Sphingobium yanoikuyae B1
    Oxford University Press (OUP) ; 2007
    In:  Journal of Industrial Microbiology & Biotechnology Vol. 34, No. 4 ( 2007-3-20), p. 311-324
    Details
    In: Journal of Industrial Microbiology & Biotechnology, Oxford University Press (OUP), Vol. 34, No. 4 ( 2007-3-20), p. 311-324
    Materialart: Online-Ressource
    ISSN: 1367-5435 , 1476-5535
    URL: Article
    DOI: 10.1007/s10295-006-0199-8
    Sprache: Englisch
    Verlag: Oxford University Press (OUP)
    Publikationsdatum: 2007
    ZDB Id: 1482484-X
    SSG: 12
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  • 3
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    Role of IncP-1β Plasmids pWDL7:: rfp and pNB8c in Chloroaniline Catabolism as Determined by Genomic and Functional Analyses
    American Society for Microbiology ; 2012
    In:  Applied and Environmental Microbiology Vol. 78, No. 3 ( 2012-02), p. 828-838
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 78, No. 3 ( 2012-02), p. 828-838
    Kurzfassung: Broad-host-range catabolic plasmids play an important role in bacterial degradation of man-made compounds. To gain insight into the role of these plasmids in chloroaniline degradation, we determined the first complete nucleotide sequences of an IncP-1 chloroaniline degradation plasmid, pWDL7:: rfp and its close relative pNB8c, as well as the expression pattern, function, and bioaugmentation potential of the putative 3-chloroaniline (3-CA) oxidation genes. Based on phylogenetic analysis of backbone proteins, both plasmids are members of a distinct clade within the IncP-1β subgroup. The plasmids are almost identical, but whereas pWDL7:: rfp carries a duplicate inverted catabolic transposon, Tn 6063 , containing a putative 3-CA oxidation gene cluster, dcaQTA1A2BR , pNB8c contains only a single copy of the transposon. No genes for an aromatic ring cleavage pathway were detected on either plasmid, suggesting that only the upper 3-CA degradation pathway was present. The dcaA1A2B gene products expressed from a high-copy-number vector were shown to convert 3-CA to 4-chlorocatechol in Escherichia coli . Slight differences in the dca promoter region between the plasmids and lack of induction of transcription of the pNB8c dca genes by 3-CA may explain previous findings that pNB8C does not confer 3-CA transformation. Bioaugmentation of activated sludge with pWDL7:: rfp accelerated removal of 3-CA, but only in the presence of an additional carbon source. Successful bioaugmentation requires complementation of the upper pathway genes with chlorocatechol cleavage genes in indigenous bacteria. The genome sequences of these plasmids thus help explain the molecular basis of their catabolic activities.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.07480-11
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2012
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
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  • 4
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    ExpR Coordinates the Expression of Symbiotically Important, Bundle-Forming Flp Pili with Quorum Sensing in Sinorhizobium meliloti
    American Society for Microbiology ; 2014
    In:  Applied and Environmental Microbiology Vol. 80, No. 8 ( 2014-04-15), p. 2429-2439
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 80, No. 8 ( 2014-04-15), p. 2429-2439
    Kurzfassung: Type IVb pili in enteropathogenic bacteria function as a host colonization factor by mediating tight adherence to host cells, but their role in bacterium-plant symbiosis is currently unknown. The genome of the symbiotic soil bacterium Sinorhizobium meliloti contains two clusters encoding proteins for type IVb pili of the Flp (fimbrial low-molecular-weight protein) subfamily. To establish the role of Flp pili in the symbiotic interaction of S. meliloti and its host, Medicago sativa , we deleted pilA1 , which encodes the putative pilin subunit in the chromosomal flp-1 cluster and conducted competitive nodulation assays. The pilA1 deletion strain formed 27% fewer nodules than the wild type. Transmission electron microscopy revealed the presence of bundle-forming pili protruding from the polar and lateral region of S. meliloti wild-type cells. The putative pilus assembly ATPase CpaE1 fused to mCherry showed a predominantly unilateral localization. Transcriptional reporter gene assays demonstrated that expression of pilA1 peaks in early stationary phase and is repressed by the quorum-sensing regulator ExpR, which also controls production of exopolysaccharides and motility. Binding of acyl homoserine lactone-activated ExpR to the pilA1 promoter was confirmed with electrophoretic mobility shift assays. A 17-bp consensus sequence for ExpR binding was identified within the 28-bp protected region by DNase I footprinting analyses. Our results show that Flp pili are important for efficient symbiosis of S. meliloti with its plant host. The temporal inverse regulation of exopolysaccharides and pili by ExpR enables S. meliloti to achieve a coordinated expression of cellular processes during early stages of host interaction.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.04088-13
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2014
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 5
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    SmoXYB1C1Z of Mycobacterium sp. Strain NBB4: a Soluble Methane Monooxygenase (sMMO)-Like Enzyme, Active on C 2 to C 4 Alkanes and Alkenes
    American Society for Microbiology ; 2014
    In:  Applied and Environmental Microbiology Vol. 80, No. 18 ( 2014-09-15), p. 5801-5806
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 80, No. 18 ( 2014-09-15), p. 5801-5806
    Kurzfassung: Monooxygenase (MO) enzymes initiate the aerobic oxidation of alkanes and alkenes in bacteria. A cluster of MO genes ( smoXYB1C1Z ) of thus-far-unknown function was found previously in the genomes of two Mycobacterium strains (NBB3 and NBB4) which grow on hydrocarbons. The predicted Smo enzymes have only moderate amino acid identity (30 to 60%) to their closest homologs, the soluble methane and butane MOs (sMMO and sBMO), and the smo gene cluster has a different organization from those of sMMO and sBMO. The smoXYB1C1Z genes of NBB4 were cloned into pMycoFos to make pSmo, which was transformed into Mycobacterium smegmatis mc 2 -155. Cells of mc 2 -155(pSmo) metabolized C 2 to C 4 alkanes, alkenes, and chlorinated hydrocarbons. The activities of mc 2 -155(pSmo) cells were 0.94, 0.57, 0.12, and 0.04 nmol/min/mg of protein with ethene, ethane, propane, and butane as substrates, respectively. The mc 2 -155(pSmo) cells made epoxides from ethene, propene, and 1-butene, confirming that Smo was an oxygenase. Epoxides were not produced from larger alkenes (1-octene and styrene). Vinyl chloride and 1,2-dichloroethane were biodegraded by cells expressing Smo, with production of inorganic chloride. This study shows that Smo is a functional oxygenase which is active against small hydrocarbons. M. smegmatis mc 2 -155(pSmo) provides a new model for studying sMMO-like monooxygenases.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.01338-14
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2014
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 6
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    Escherichia coli Enoyl-Acyl Carrier Protein Reductase (FabI) Supports Efficient Operation of a Functional Reversal of the β-Oxidation Cycle
    American Society for Microbiology ; 2015
    In:  Applied and Environmental Microbiology Vol. 81, No. 4 ( 2015-02-15), p. 1406-1416
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 81, No. 4 ( 2015-02-15), p. 1406-1416
    Kurzfassung: We recently used a synthetic/bottom-up approach to establish the identity of the four enzymes composing an engineered functional reversal of the β-oxidation cycle for fuel and chemical production in Escherichia coli (J. M. Clomburg, J. E. Vick, M. D. Blankschien, M. Rodriguez-Moya, and R. Gonzalez, ACS Synth Biol 1:541–554, 2012, http://dx.doi.org/10.1021/sb3000782 ). While native enzymes that catalyze the first three steps of the pathway were identified, the identity of the native enzyme(s) acting as the trans -enoyl coenzyme A (CoA) reductase(s) remained unknown, limiting the amount of product that could be synthesized (e.g., 0.34 g/liter butyrate) and requiring the overexpression of a foreign enzyme (the Euglena gracilis trans -enoyl-CoA reductase [ Eg TER]) to achieve high titers (e.g., 3.4 g/liter butyrate). Here, we examine several native E. coli enzymes hypothesized to catalyze the reduction of enoyl-CoAs to acyl-CoAs. Our results indicate that FabI, the native enoyl-acyl carrier protein (enoyl-ACP) reductase (ENR) from type II fatty acid biosynthesis, possesses sufficient NADH-dependent TER activity to support the efficient operation of a β-oxidation reversal. Overexpression of FabI proved as effective as Eg TER for the production of butyrate and longer-chain carboxylic acids. Given the essential nature of fabI , we investigated whether bacterial ENRs from other families were able to complement a fabI deletion without promiscuous reduction of crotonyl-CoA. These characteristics from Bacillus subtilis FabL enabled Δ fabI complementation experiments that conclusively established that FabI encodes a native enoyl-CoA reductase activity that supports the β-oxidation reversal in E. coli .
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.03521-14
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2015
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
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  • 7
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    Inhibitory Effects of C 2 to C 10 1-Alkynes on Ammonia Oxidation in Two Nitrososphaera Species
    American Society for Microbiology ; 2015
    In:  Applied and Environmental Microbiology Vol. 81, No. 6 ( 2015-03-15), p. 1942-1948
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 81, No. 6 ( 2015-03-15), p. 1942-1948
    Kurzfassung: A previous study showed that ammonia oxidation by the Thaumarchaeota Nitrosopumilus maritimus (group 1.1a) was resistant to concentrations of the C 8 1-alkyne, octyne, which completely inhibits activity by ammonia-oxidizing bacteria. In this study, the inhibitory effects of octyne and other C 2 to C 10 1-alkynes were evaluated on the nitrite production activity of two pure culture isolates from Thaumarchaeota group 1.1b, Nitrososphaera viennensis strain EN76 and Nitrososphaera gargensis . Both N. viennensis and N. gargensis were insensitive to concentrations of octyne that cause complete and irreversible inactivation of nitrite production by ammonia-oxidizing bacteria. However, octyne concentrations (≥20 μM) that did not inhibit N. maritimus partially inhibited nitrite production in N. viennensis and N. gargensis in a manner that did not show the characteristics of irreversible inactivation. In contrast to previous studies with an ammonia-oxidizing bacterium, Nitrosomonas europaea , octyne inhibition of N. viennensis was: (i) fully and immediately reversible, (ii) not competitive with NH 4 + , and (iii) without effect on the competitive interaction between NH 4 + and acetylene. Both N. viennensis and N. gargensis demonstrated the same overall trend in regard to 1-alkyne inhibition as previously observed for N. maritimus , being highly sensitive to ≤C 5 alkynes and more resistant to longer-chain length alkynes. Reproducible differences were observed among N. maritimus , N. viennensis , and N. gargensis in regard to the extent of their resistance/sensitivity to C 6 and C 7 1-alkynes, which may indicate differences in the ammonia monooxygenase binding and catalytic site(s) among the Thaumarchaeota .
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.03688-14
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2015
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
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  • 8
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    Characterization of the Vibrio fischeri Fatty Acid Chemoreceptors, VfcB and VfcB2
    American Society for Microbiology ; 2016
    In:  Applied and Environmental Microbiology Vol. 82, No. 2 ( 2016-01-15), p. 696-704
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 82, No. 2 ( 2016-01-15), p. 696-704
    Kurzfassung: Bacteria use a wide variety of methyl-accepting chemotaxis proteins (MCPs) to mediate their attraction to or repulsion from different chemical signals in their environment. The bioluminescent marine bacterium Vibrio fischeri is the monospecific symbiont of the Hawaiian bobtail squid, Euprymna scolopes , and encodes a large repertoire of MCPs that are hypothesized to be used during different parts of its complex, multistage lifestyle. Here, we report the initial characterization of two such MCPs from V. fischeri that are responsible for mediating migration toward short- and medium-chain aliphatic (or fatty) acids. These receptors appear to be distributed among only members of the family Vibrionaceae and are likely descended from a receptor that has been lost by the majority of the members of this family. While chemotaxis greatly enhances the efficiency of host colonization by V. fischeri , fatty acids do not appear to be used as a chemical cue during this stage of the symbiosis. This study presents an example of straight-chain fatty acid chemoattraction and contributes to the growing body of characterized MCP-ligand interactions.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.02856-15
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2016
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
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  • 9
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    Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5
    American Society for Microbiology ; 2016
    In:  Applied and Environmental Microbiology Vol. 82, No. 20 ( 2016-10-15), p. 6080-6090
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 82, No. 20 ( 2016-10-15), p. 6080-6090
    Kurzfassung: Polyester polyurethane (PU) coatings are widely used to help protect underlying structural surfaces but are susceptible to biological degradation. PUs are susceptible to degradation by Pseudomonas species, due in part to the degradative activity of secreted hydrolytic enzymes. Microorganisms often respond to environmental cues by secreting enzymes or secondary metabolites to benefit their survival. This study investigated the impact of exposing several Pseudomonas strains to select carbon sources on the degradation of the colloidal polyester polyurethane Impranil DLN (Impranil). The prototypic Pseudomonas protegens strain Pf-5 exhibited Impranil-degrading activities when grown in sodium citrate but not in glucose-containing medium. Glucose also inhibited the induction of Impranil-degrading activity by citrate-fed Pf-5 in a dose-dependent manner. Biochemical and mutational analyses identified two extracellular lipases present in the Pf-5 culture supernatant (PueA and PueB) that were involved in degradation of Impranil. Deletion of the pueA gene reduced Impranil-clearing activities, while pueB deletion exhibited little effect. Removal of both genes was necessary to stop degradation of the polyurethane. Bioinformatic analysis showed that putative Cbr/Hfq/Crc-mediated regulatory elements were present in the intergenic sequences upstream of both pueA and pueB genes. Our results confirmed that both PueA and PueB extracellular enzymes act in concert to degrade Impranil. Furthermore, our data showed that carbon sources in the growth medium directly affected the levels of Impranil-degrading activity but that carbon source effects varied among Pseudomonas strains. This study uncovered an intricate and complicated regulation of P. protegens PU degradation activity controlled by carbon catabolite repression. IMPORTANCE Polyurethane (PU) coatings are commonly used to protect metals from corrosion. Microbiologically induced PU degradation might pose a substantial problem for the integrity of these coatings. Microorganisms from diverse genera, including pseudomonads, possess the ability to degrade PUs via various means. This work identified two extracellular lipases, PueA and PueB, secreted by P. protegens strain Pf-5, to be responsible for the degradation of a colloidal polyester PU, Impranil. This study also revealed that the expression of the degradative activity by strain Pf-5 is controlled by glucose carbon catabolite repression. Furthermore, this study showed that the Impranil-degrading activity of many other Pseudomonas strains could be influenced by different carbon sources. This work shed light on the carbon source regulation of PU degradation activity among pseudomonads and identified the polyurethane lipases in P. protegens .
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.01448-16
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2016
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
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  • 10
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    Enhancing Terpene Yield from Sugars via Novel Routes to 1-Deoxy- d -Xylulose 5-Phosphate
    American Society for Microbiology ; 2015
    In:  Applied and Environmental Microbiology Vol. 81, No. 1 ( 2015-01), p. 130-138
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 81, No. 1 ( 2015-01), p. 130-138
    Kurzfassung: Terpene synthesis in the majority of bacterial species, together with plant plastids, takes place via the 1-deoxy- d -xylulose 5-phosphate (DXP) pathway. The first step of this pathway involves the condensation of pyruvate and glyceraldehyde 3-phosphate by DXP synthase (Dxs), with one-sixth of the carbon lost as CO 2 . A hypothetical novel route from a pentose phosphate to DXP (nDXP) could enable a more direct pathway from C 5 sugars to terpenes and also circumvent regulatory mechanisms that control Dxs, but there is no enzyme known that can convert a sugar into its 1-deoxy equivalent. Employing a selection for complementation of a dxs deletion in Escherichia coli grown on xylose as the sole carbon source, we uncovered two candidate nDXP genes. Complementation was achieved either via overexpression of the wild-type E. coli yajO gene, annotated as a putative xylose reductase, or via various mutations in the native ribB gene. In vitro analysis performed with purified YajO and mutant RibB proteins revealed that DXP was synthesized in both cases from ribulose 5-phosphate (Ru5P). We demonstrate the utility of these genes for microbial terpene biosynthesis by engineering the DXP pathway in E. coli for production of the sesquiterpene bisabolene, a candidate biodiesel. To further improve flux into the pathway from Ru5P, nDXP enzymes were expressed as fusions to DXP reductase (Dxr), the second enzyme in the DXP pathway. Expression of a Dxr-RibB(G108S) fusion improved bisabolene titers more than 4-fold and alleviated accumulation of intracellular DXP.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.02920-14
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2015
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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