Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: Comparative 13C NMR analysis of the products in wild-type and mutants

Choi, M. Y.; Xu, Jinbang; García-Gutiérrez, Mari Cruz; Yoo, Taesik; Cho, You‐Hee; Yoon, Sung Chul

doi:10.1016/j.jbiotec.2010.10.072

Cited by 44 publications

(30 citation statements)

References 36 publications

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“…4), it is clear that S is regulating nutrient homeostasis during the PHB cycle. RpoS was shown previously to have a role in polyhydroxyalkanoate (PHA) biosynthesis in Pseudomonas oleovorans (16,50). However, in Pseudomonas putida, an rpoS mutation resulted in an increased PHA degradation rate (46), similar to what was observed in this study.…”

Section: Discussionsupporting

confidence: 86%

Whole-Genome Microarray and Gene Deletion Studies Reveal Regulation of the Polyhydroxyalkanoate Production Cycle by the Stringent Response in Ralstonia eutropha H16

Brigham

Speth

Rha

et al. 2012

Appl Environ Microbiol

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bPoly(3-hydroxybutyrate) (PHB) production and mobilization in Ralstonia eutropha are well studied, but in only a few instances has PHB production been explored in relation to other cellular processes. We examined the global gene expression of wild-type R. eutropha throughout the PHB cycle: growth on fructose, PHB production using fructose following ammonium depletion, and PHB utilization in the absence of exogenous carbon after ammonium was resupplied. Our results confirm or lend support to previously reported results regarding the expression of PHB-related genes and enzymes. Additionally, genes for many different cellular processes, such as DNA replication, cell division, and translation, are selectively repressed during PHB production. In contrast, the expression levels of genes under the control of the alternative sigma factor 54 increase sharply during PHB production and are repressed again during PHB utilization. Global gene regulation during PHB production is strongly reminiscent of the gene expression pattern observed during the stringent response in other species. Furthermore, a ppGpp synthase deletion mutant did not show an accumulation of PHB, and the chemical induction of the stringent response with DL-norvaline caused an increased accumulation of PHB in the presence of ammonium. These results indicate that the stringent response is required for PHB accumulation in R. eutropha, helping to elucidate a thus-far-unknown physiological basis for this process.

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Section: Discussionsupporting

confidence: 86%

Whole-Genome Microarray and Gene Deletion Studies Reveal Regulation of the Polyhydroxyalkanoate Production Cycle by the Stringent Response in Ralstonia eutropha H16

Brigham

Speth

Rha

et al. 2012

Appl Environ Microbiol

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“…A clear example is the enhanced rhamnolipid production in polyhydroxyalkanoate (PHA)-deficient mutants of B. thailandensis (Funston et al 2017). Contrarily, PHA-deficient mutants of P. aeruginosa did not produce significantly higher rhamnolipid yields compared to wild type; however, rhamnolipid-deficient mutants produced significantly higher yields of PHA (Choi et al 2011). …”

Section: Discussionmentioning

confidence: 99%

Fatty acid synthesis pathway provides lipid precursors for rhamnolipid biosynthesis in Burkholderia thailandensis E264

Irorere

Smyth

Cobice

et al. 2018

Appl Microbiol Biotechnol

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Rhamnolipid production was monitored for a period of 216 h using different substrates in Pseudomonas aeruginosa PAO1 and Burkholderia thailandensis E264 which showed comparable crude yields attained by both after 216 h. The crude yield for P. aeruginosa, however, was significantly higher at the early stages of fermentation (72 or 144 h). Additionally, P. aeruginosa produced rhamnolipid with odd and even carbon chain lipid moieties using odd carbon chain fatty acid substrates (up to 45.97 and 67.57%, respectively). In contrast, B. thailandensis produced rhamnolipid with predominantly even carbon chain lipid moieties (up to 99.26). These results indicate the use of the fatty acid synthesis (FAS II) pathway as the main source of lipid precursors in rhamnolipid biosynthesis by B. thailandensis. Isotope tracing using 0.25% stearic acid – d35 + 1% glycerol as carbon substrate showed a single pattern of deuterium incorporation: with predominantly less than 15 deuterium atoms incorporated into a single Di-C14-C14 rhamnolipid molecule. This further indicates that the FAS II pathway is the main source of the lipid precursor in rhamnolipid biosynthesis by B. thailandensis. The pathogenicity of these strains was also assessed, and results showed that B. thailandensis is significantly less pathogenic than P. aeruginosa with an LC50 at 24 h > 2500, approximately three logs higher than P. aeruginosa using the Galleria mellonella larva model.Electronic supplementary materialThe online version of this article (10.1007/s00253-018-9059-5) contains supplementary material, which is available to authorized users.

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“…Thus, in those pseudomonads which are able to accumulate PHA MCL and secrete RL, both biosynthesis pathways compete for the same precursors. This becomes obvious in mutants defective in RL synthesis, as they show elevated PHA MCL accumulation (300,301). Figure 21 illustrates the biosynthesis of mono-or dirhamnolipids from 3-hydroxyacyl-ACPs derived from de novo fatty acid synthesis.…”

Section: Rhamnolipid Biosynthesismentioning

confidence: 99%

Acyltransferases in Bacteria

Röttig

Steinbüchel

2013

Microbiol Mol Biol Rev

151

141

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SUMMARY Long-chain-length hydrophobic acyl residues play a vital role in a multitude of essential biological structures and processes. They build the inner hydrophobic layers of biological membranes, are converted to intracellular storage compounds, and are used to modify protein properties or function as membrane anchors, to name only a few functions. Acyl thioesters are transferred by acyltransferases or transacylases to a variety of different substrates or are polymerized to lipophilic storage compounds. Lipases represent another important enzyme class dealing with fatty acyl chains; however, they cannot be regarded as acyltransferases in the strict sense. This review provides a detailed survey of the wide spectrum of bacterial acyltransferases and compares different enzyme families in regard to their catalytic mechanisms. On the basis of their studied or assumed mechanisms, most of the acyl-transferring enzymes can be divided into two groups. The majority of enzymes discussed in this review employ a conserved acyltransferase motif with an invariant histidine residue, followed by an acidic amino acid residue, and their catalytic mechanism is characterized by a noncovalent transition state. In contrast to that, lipases rely on completely different mechanism which employs a catalytic triad and functions via the formation of covalent intermediates. This is, for example, similar to the mechanism which has been suggested for polyester synthases. Consequently, although the presented enzyme types neither share homology nor have a common three-dimensional structure, and although they deal with greatly varying molecule structures, this variety is not reflected in their mechanisms, all of which rely on a catalytically active histidine residue.

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Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: Comparative 13C NMR analysis of the products in wild-type and mutants

Cited by 44 publications

References 36 publications

Whole-Genome Microarray and Gene Deletion Studies Reveal Regulation of the Polyhydroxyalkanoate Production Cycle by the Stringent Response in Ralstonia eutropha H16

Whole-Genome Microarray and Gene Deletion Studies Reveal Regulation of the Polyhydroxyalkanoate Production Cycle by the Stringent Response in Ralstonia eutropha H16

Fatty acid synthesis pathway provides lipid precursors for rhamnolipid biosynthesis in Burkholderia thailandensis E264

Acyltransferases in Bacteria

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