The oxalic acid biosynthetic activity of Burkholderia mallei is encoded by a single locus

Nakata, Paul A.

doi:10.1016/j.micres.2010.11.002

Cited by 22 publications

(28 citation statements)

References 17 publications

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“…4C). In B. thailandensis and B. pseudomallei, a single Obc homolog, Obc1, is predicted to be responsible for oxalate biosynthesis (20). The N terminus of Obc1 shares 54% amino acid identity with full-length ObcA, whereas the C terminus of Obc1 has no similarity with ObcA or ObcB (Fig.…”

Section: Microbiologymentioning

confidence: 99%

Bacterial quorum sensing, cooperativity, and anticipation of stationary-phase stress

Goo

Majerczyk

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

112

169

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Acyl-homoserine lactone-mediated quorum sensing (QS) regulates diverse activities in many species of Proteobacteria. QS-controlled genes commonly code for production of secreted or excreted public goods. The acyl-homoserine lactones are synthesized by members of the LuxI signal synthase family and are detected by cognate members of the LuxR family of transcriptional regulators. QS affords a means of population density-dependent gene regulation. Control of public goods via QS provides a fitness benefit. Another potential role for QS is to anticipate overcrowding. As population density increases and stationary phase approaches, QS might induce functions important for existence in stationary phase. Here we provide evidence that in three related species of the genus Burkholderia QS allows individuals to anticipate and survive stationary-phase stress. Survival requires QS-dependent activation of cellular enzymes required for production of excreted oxalate, which serves to counteract ammonia-mediated alkaline toxicity during stationary phase. Our findings provide an example of QS serving as a means to anticipate stationary phase or life at the carrying capacity of a population by activating the expression of cytoplasmic enzymes, altering cellular metabolism, and producing a shared resource or public good, oxalate.Burkholderia carrying capacity | glumae | pseudomallei | thailandensis | cell death A cyl-homoserine lactone (AHL)-mediated quorum sensing (QS) regulates diverse activities, including bioluminescence, biofilm formation, motility, and virulence factor formation, in many Proteobacteria (1-3). AHLs are synthesized most typically by members of the LuxI family signal synthases and detected by members of the LuxR family of transcriptional regulators (1-3). A large body of work has characterized the molecular mechanisms of bacterial QS; demonstrating the population-wide benefits that drive QS-mediated cooperative behavior has proven difficult, however. Cooperative activities benefit individuals within a group (4, 5).QS-controlled genes commonly code for the production of extracellular public goods that can be shared by all members of the group regardless of which members produce them. These extracellular products are often important for nutrient acquisition, interspecies competition, or virulence (6-8). In Pseudomonas aeruginosa, QS control of secreted proteases provides fitness benefits, because the proteases are produced only when they can be used efficiently (9). Other potential roles of QS in bacteria have been proposed, including the hypothesis that QS enables bacteria to anticipate population carrying capacity in a given environment. Anticipation of stationary phase might allow individuals to modify their physiology in preparation for survival at population carrying capacity.Here we address the question of whether QS is involved in anticipation of stationary-phase stress in three closely related bacteria: the rice pathogen Burkholderia glumae, the opportunistic human pathogen Burkholderia pseudomallei, and the...

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Section: Microbiologymentioning

confidence: 99%

Bacterial quorum sensing, cooperativity, and anticipation of stationary-phase stress

Goo

Majerczyk

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

112

169

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“…Cloning and Purification of Wild-type Obc1 and Its Mutants-The gene for Obc1 from B. thailandensis (7,11) was amplified by colony PCR and cloned into a modified pET28b expression vector (Merck) containing a tobacco etch virus protease recognition sequence between the His 5 tag and multiple cloning site. The resulting plasmid containing N-terminal Histagged Obc1 was transformed into Escherichia coli BL21 (DE3) cells (Novagen).…”

Section: Methodsmentioning

confidence: 99%

“…1A). Interestingly, in Burkholderia thailandensis, Burkholderia pseudomallei, and Burkholderia mallei, the bifunctional enzyme Obc1 catalyzes these two reactions (11). Given that Obc1 functionally complements ObcA and ObcB, it is not surprising that it contains activities of both enzymes.…”

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confidence: 99%

“…Given that Obc1 functionally complements ObcA and ObcB, it is not surprising that it contains activities of both enzymes. The N-terminal domain of Obc1 exhibits 52% identity with the amino acid sequence of ObcA (10,11) (Fig. 2); however, the Obc1 C-terminal domain does not show any sequence homology with ObcB even though it exhibits functional identity with ObcB.…”

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confidence: 99%

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Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity

Hwang

Rhee

2016

Journal of Biological Chemistry

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In Burkholderia species, the production of oxalate, an acidic molecule, is a key event for bacterial growth in the stationary phase. Oxalate plays a central role in maintaining environmental pH, which counteracts inevitable population-collapsing alkaline toxicity in amino acid-based culture medium. In the phytopathogen Burkholderia glumae, two enzymes are responsible for oxalate production. First, the enzyme oxalate biosynthetic component A (ObcA) catalyzes the formation of a tetrahedral C6-CoA adduct from the substrates acetyl-CoA and oxaloacetate. Then the ObcB enzyme liberates three products from the C6-CoA adduct: oxalate, acetoacetate, and CoA. Interestingly, these two stepwise reactions are catalyzed by a single bifunctional enzyme, Obc1, from Burkholderia thailandensis and Burkholderia pseudomallei. Obc1 has an ObcA-like N-terminal domain and shows ObcB activity in its C-terminal domain despite no sequence homology with ObcB. We report the crystal structure of Obc1 in its apo and glycerol-bound form at 2.5 Å and 2.8 Å resolution, respectively. The Obc1 N-terminal domain is essentially identical both in structure and function to that of ObcA. Its C-terminal domain has an ␣/␤ hydrolase fold that has a catalytic triad for oxalate production and a novel oxyanion hole distinct from the canonical HGGG motif in other ␣/␤ hydrolases. Functional analyses through mutagenesis studies suggested that His-934 is an additional catalytic acid/base for its lyase activity and liberates two additional products, acetoacetate and CoA. These results provide structural and functional insights into bacterial oxalogenesis and an example of divergent evolution of the ␣/␤ hydrolase fold, which has both hydrolase and lyase activity.

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“…Unlike B. glumae, B. thailandensis catalyzes the two-step reaction with a single bifunctional enzyme, Obc1, which consists of an ObcA homolog (54% sequence identity) in its N-terminal domain (see Fig. 2) and a functional ObcB-like enzyme, with no apparent sequence homology to ObcB, in its C-terminal domain (14).…”

Section: )mentioning

confidence: 99%

Structural basis for bacterial quorum sensing-mediated oxalogenesis

Goo

Hwang

et al. 2014

Acta Cryst Sect A

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Background: Oxalogenesis in the Burkholderia species is an indispensable event for their survival in the stationary phase. Results: Structural and functional analyses of ObcA, the first enzyme in oxalogenesis, unravel an unprecedented reaction mechanism. Conclusion: ObcA produces a tetrahedral CoA adduct. Significance: This study provides a structural basis for understanding the first step in oxalogenesis.

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The oxalic acid biosynthetic activity of Burkholderia mallei is encoded by a single locus

Cited by 22 publications

References 17 publications

Bacterial quorum sensing, cooperativity, and anticipation of stationary-phase stress

Bacterial quorum sensing, cooperativity, and anticipation of stationary-phase stress

Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity

Structural basis for bacterial quorum sensing-mediated oxalogenesis

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