Inhibition by temperature of the terminal step in biosynthesis of prodigiosin

Williams, Robert P.; Goldschmidt, Millicent E.; Gott, Cora L.

doi:10.1016/0006-291x(65)90500-0

Cited by 38 publications

(15 citation statements)

References 5 publications

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“…A bifurcated pathway has been proposed for the biosynthesis of prodigiosin culminating in the enzymic condensation of the terminal products of the two pathways, 4-methoxy-2,2 ¢ -bipyrrole-5-carbaldehyde (MBC) and 2-methyl-3-n-amyl-pyrrole (MAP) (Harris et al ., 2004). Although the condensation reaction can occur spontaneously at low pH, in bacteria this reaction occurs by a temperature-sensitive enzymatic reaction (Rapoport and Holden, 1962;Williams et al ., 1965;Fürstner, 2003). The precursors for prodigiosin were shown to be acetate, serine, alanine, methionine and proline (Williams, 1973).…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2‐methyl‐3‐n‐amyl‐pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces

Williamson

Simonsen

Ahmed

et al. 2005

Molecular Microbiology

211

241

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SummaryThe biosynthetic pathway of the red-pigmented antibiotic, prodigiosin, produced by Serratia sp. is known to involve separate pathways for the production of the monopyrrole, 2-methyl-3-n-amyl-pyrrole (MAP) and the bipyrrole, 4-methoxy-2,2 ¢ -bipyrrole-5-carbaldehyde (MBC) which are then coupled in the final condensation step. We have previously reported the cloning, sequencing and heterologous expression of the pig cluster responsible for prodigiosin biosynthesis in two Serratia sp. In this article we report the creation of in-frame deletions or insertions in every biosynthetic gene in the cluster from Serratia sp. ATCC 39006. The biosynthetic intermediates accumulating in each mutant have been analysed by LC-MS, cross-feeding and genetic complementation studies. Based on these results we assign specific roles in the biosynthesis of MBC to the following Pig proteins: PigI, PigG, PigA, PigJ, PigH, PigM, PigF and PigN. We report a novel pathway for the biosynthesis of MAP, involving PigD, PigE and PigB. We also report a new chemical synthesis of MAP and one of its precursors, 3-acetyloctanal. Finally, we identify the condensing enzyme as PigC. We reassess the existing literature and discuss the significance of the results for the biosynthesis of undecylprodigiosin by the Red cluster in Streptomyces coelicolor A3(2).

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Section: Introductionmentioning

confidence: 99%

Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2‐methyl‐3‐n‐amyl‐pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces

Williamson

Simonsen

Ahmed

et al. 2005

Molecular Microbiology

211

241

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“…Prodigiosin production by S. marcescens and other Serratia species is regulated by a number of physiological and environmental factors, including, but not limited to, growth phase, temperature (56,57), pH (50), oxygen concentration (24), and nutrient and mineral content of the medium (4,15,21,49,60).…”

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confidence: 99%

Serratia marcescens Quinoprotein Glucose Dehydrogenase Activity Mediates Medium Acidification and Inhibition of Prodigiosin Production by Glucose

Fender

Bender

Stella

et al. 2012

Appl Environ Microbiol

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ABSTRACTSerratia marcescensis a model organism for the study of secondary metabolites. The biologically active pigment prodigiosin (2-methyl-3-pentyl-6-methoxyprodiginine), like many other secondary metabolites, is inhibited by growth in glucose-rich medium. Whereas previous studies indicated that this inhibitory effect was pH dependent and did not require cyclic AMP (cAMP), there is no information on the genes involved in mediating this phenomenon. Here we used transposon mutagenesis to identify genes involved in the inhibition of prodigiosin by glucose. Multiple genetic loci involved in quinoprotein glucose dehydrogenase (GDH) activity were found to be required for glucose inhibition of prodigiosin production, including pyrroloquinoline quinone and ubiquinone biosynthetic genes. Upon assessing whether the enzymatic products of GDH activity were involved in the inhibitory effect, we observed thatd-glucono-1,5-lactone andd-gluconic acid, but notd-gluconate, were able to inhibit prodigiosin production. These data support a model in which the oxidation ofd-glucose by quinoprotein GDH initiates a reduction in pH that inhibits prodigiosin production through transcriptional control of the prodigiosin biosynthetic operon, providing new insight into the genetic pathways that control prodigiosin production. Strains generated in this report may be useful in large-scale production of secondary metabolites.

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“…Genes encoding parts of the biosynthetic pathway have recently been cloned in Escherichia coli (3). The terminal step in prodigiosin biosynthesis (condensing of mono-and bipyrrole moieties) is temperature sensitive (24). The function of this water-insoluble pigment in S. marcescens is not clear.…”

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Flagellar variation in Serratia marcescens is associated with color variation

Paruchuri¹,

Harshey

1987

J Bacteriol

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The pigmented enterobacterium Serratia marcescens, an opportunistic pathogen, shows a striking variation of its red color. Different strains differ greatly both in color and in the frequency with which they produce color variants. Within a strain, the variations occur at constant rates and are reversible. During an investigation of this phenomenon we observed that variation of a 39-kilodalton protein in S. marcescens 274 is closely associated with color variation. Using antibodies to this protein we identified it as being a component of the bacterial flagella. Variation of surface proteins often provides an organism with alternate offense-defense strategies for survival in a challenging environment. The pigment, in association with flagella, may provide such a function for S. marcescens.

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Inhibition by temperature of the terminal step in biosynthesis of prodigiosin

Cited by 38 publications

References 5 publications

Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2‐methyl‐3‐n‐amyl‐pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces

Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2‐methyl‐3‐n‐amyl‐pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces

Serratia marcescens Quinoprotein Glucose Dehydrogenase Activity Mediates Medium Acidification and Inhibition of Prodigiosin Production by Glucose

Flagellar variation in Serratia marcescens is associated with color variation

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