Indole toxicity involves the inhibition of adenosine triphosphate production and protein folding in<i>Pseudomonas putida</i>

Kim, Jisun; Hong, Hyerim; Heo, Aram; Park, Woojun

doi:10.1111/1574-6968.12135

Cited by 50 publications

(42 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The structures of the bioconversion products were determined using 1 H nuclear magnetic resonance (NMR) and 13 C NMR. 1 H NMR spectra were recorded in hexadeuterodimethyl sulfoxide (DMSO-D 6 ) or CDCl 3 on a Bruker Ascend 400 at 400 MHz, and 13 C NMR spectra were recorded on a Bruker Ascend 400 at 100 MHz.…”

Section: Methodsmentioning

confidence: 99%

“…Toxic indole concentrations reportedly vary for different microorganisms in the range of 0.5 to 5 mM (11). The main mechanisms of indole toxicity are reported to be an alteration of membrane potential with subsequent inhibition of cell division (12), depletion of ATP levels (13), and an inhibition of acyl-homoserine lactone (AHL)-based quorum sensing by regulator misfolding (14).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization

Sadauskas

Vaitekūnas

Gasparavičiūtė

et al. 2017

Appl Environ Microbiol

View full text Add to dashboard Cite

Indole is a molecule of considerable biochemical significance, acting as both an interspecies signal molecule and a building block of biological elements. Bacterial indole degradation has been demonstrated for a number of cases; however, very little is known about genes and proteins involved in this process. This study reports the cloning and initial functional characterization of genes (iif and ant cluster) responsible for indole biodegradation in Acinetobacter sp. strain O153. The catabolic cascade was reconstituted in vitro with recombinant proteins, and each protein was assigned an enzymatic function. Degradation starts with oxidation, mediated by the IifC and IifD flavin-dependent two-component oxygenase system. Formation of indigo is prevented by IifB, and the final product, anthranilic acid, is formed by IifA, an enzyme which is both structurally and functionally comparable to cofactor-independent oxygenases. Moreover, the iif cluster was identified in the genomes of a wide range of bacteria, suggesting the potential of widespread Iifmediated indole degradation. This work provides novel insights into the genetic background of microbial indole biodegradation.IMPORTANCE The key finding of this research is identification of the genes responsible for microbial biodegradation of indole, a toxic N-heterocyclic compound. A large amount of indole is present in urban wastewater and sewage sludge, creating a demand for an efficient and eco-friendly means to eliminate this pollutant. A common strategy of oxidizing indole to indigo has the major drawback of producing insoluble material. Genes and proteins of Acinetobacter sp. strain O153 (DSM 103907) reported here pave the way for effective and indigo-free indole removal. In addition, this work suggests possible novel means of indole-mediated bacterial interactions and provides the basis for future research on indole metabolism. KEYWORDS indole, biodegradation, bacterial metabolism, Acinetobacter, bacterial signaling, cofactor-independent oxygenases I ndole is an N-heterocyclic aromatic compound derived mainly by TnaA tryptophanase from L-tryptophan in Escherichia coli (1) and is widely found in natural environments. Indole acts as cell-to-cell signaling molecule that regulates the expression of several virulence genes (2-4), promotes biofilm formation (5-7), and mediates complex predator-prey interactions (8, 9). At high concentrations, indole and its derivatives exhibit toxic activity to both prokaryotic cells and animals and are even considered mutagens (10). Toxic indole concentrations reportedly vary for different microorganisms in the range of 0.5 to 5 mM (11). The main mechanisms of indole toxicity are reported to be an alteration of membrane potential with subsequent inhibition of cell division (12), depletion of ATP levels (13), and an inhibition of acyl-homoserine lactone (AHL)-based quorum sensing by regulator misfolding (14).In order to utilize aromatic compounds as an energy source, microorganisms have

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization

Sadauskas

Vaitekūnas

Gasparavičiūtė

et al. 2017

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…To confirm ATP concentrations, exponentially growing cultures were treated with 0.5 mM or 1 mM PQ for 15 min, and cells were harvested for ATP extraction using 1% trichloroacetic acid buffer and treated as previously described (22). The ATP concentration is expressed as the molar concentration per mg of protein.…”

Section: Gene Expression Analysis Using Real-time Rt-pcr (Qrt-pcr)-mentioning

confidence: 99%

“…Exponentially growing cultures were treated with 1 mM PQ for 15 min, and cells were collected for NADH and NAD ϩ extraction. Further procedures were performed as previously described (22). NAD ϩ and NADH concentrations were normalized by the amount of total protein.…”

Section: Measurement Of the Nadh/nadmentioning

confidence: 99%

Role of Glyoxylate Shunt in Oxidative Stress Response

Ahn

Jung

Jang

et al. 2016

Journal of Biological Chemistry

Self Cite

200

161

View full text Add to dashboard Cite

The glyoxylate shunt (GS) is a two-step metabolic pathway (isocitrate lyase, aceA; and malate synthase, glcB) that serves as an alternative to the tricarboxylic acid cycle. The GS bypasses the carbon dioxide-producing steps of the tricarboxylic acid cycle and is essential for acetate and fatty acid metabolism in bacteria. GS can be up-regulated under conditions of oxidative stress, antibiotic stress, and host infection, which implies that it plays important but poorly explored roles in stress defense and pathogenesis. In many bacterial species, including Pseudomonas aeruginosa, aceA and glcB are not in an operon, unlike in Escherichia coli. In P. aeruginosa, we explored relationships between GS genes and growth, transcription profiles, and biofilm formation. Contrary to our expectations, deletion of aceA in P. aeruginosa improved cell growth under conditions of oxidative and antibiotic stress. Transcriptome data suggested that aceA mutants underwent a metabolic shift toward aerobic denitrification; this was supported by additional evidence, including up-regulation of denitrification-related genes, decreased oxygen consumption without lowering ATP yield, increased production of denitrification intermediates (NO and N 2 O), and increased cyanide resistance. The aceA mutants also produced a thicker exopolysaccharide layer; that is, a phenotype consistent with aerobic denitrification. A bioinformatic survey across known bacterial genomes showed that only microorganisms capable of aerobic metabolism possess the glyoxylate shunt. This trend is consistent with the hypothesis that the GS plays a previously unrecognized role in allowing bacteria to tolerate oxidative stress.

show abstract

“…strain In3 [19]. Similarly, cell growth and indole degradation by Pseudomonas aeruginosa Gs were inhibited when the concentration of indole was 4.0 mM [22], and Pseudomonas putida KT2440 cells did not grow well at above 3 mM indole [24].…”

Section: Discussionmentioning

confidence: 97%

Isolation of Indole Utilizing Bacteria Arthrobacter sp. and Alcaligenes sp. From Livestock Waste

et al. 2016

View full text Add to dashboard Cite

Indole is an interspecies and interkingdom signaling molecule widespread in different environmental compartment. Although multifaceted roles of indole in different biological systems have been established, little information is available on the microbial utilization of indole in the context of combating odor emissions from different types of waste. The present study was aimed at identifying novel bacteria capable of utilizing indole as the sole carbon and energy source. From the selective enrichment of swine waste and cattle feces, we identified Gram-positive and Gramnegative bacteria belonging to the genera Arthrobacter and Alcaligenes. Bacteria belonging to the genus Alcaligenes showed higher rates of indole utilization than Arthrobacter. Indole at 1.0 mM for growth was completely utilized by Alcaligenes sp. in 16 h. Both strains produced two intermediates, anthranilic acid and isatin, during aerobic indole metabolism. These isolates were also able to grow on several indole derivatives. Interestingly, an adaptive response in terms of a decrease in cell size was observed in both strains in the presence of indole. The present study will help to explain the degradation of indole by different bacteria and also the pathways through which it is catabolized. Furthermore, these novel bacterial isolates could be potentially useful for the in situ attenuation of odorant indole and its derivatives emitted from different types of livestock waste.

show abstract

Indole toxicity involves the inhibition of adenosine triphosphate production and protein folding inPseudomonas putida

Cited by 50 publications

References 44 publications

Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization

Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization

Role of Glyoxylate Shunt in Oxidative Stress Response

Isolation of Indole Utilizing Bacteria Arthrobacter sp. and Alcaligenes sp. From Livestock Waste

Contact Info

Product

Resources

About