Dimethylformamide is a novel nitrilase inducer in Rhodococcus rhodochrous

Chhiba-Govindjee, Varsha P; Mathiba, Kgama; Westhuyzen, Christiaan W. van der; Steenkamp, Paul A.; Rashamuse, J. K.; Stoychev, Stoyan; Bode, Moira L.; Brady, Dean

doi:10.1007/s00253-018-9367-9

Cited by 20 publications

(17 citation statements)

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“…The alternative nitrile hydrolysis enzyme, nitrilase, is also found in R. rhodochrous ATCC BAA-870. It expresses an enantioselective aliphatic nitrilase encoded on the plasmid, which is induced by dimethylformamide [37]. Another nitrilase/cyanide hydratase family protein is also annotated on the plasmid (this study) but has not been characterised.…”

Section: Resultsmentioning

confidence: 99%

“…These enzymes can also perform enantioselective hydrolysis of nitrile compounds selected from classes of chemicals used in pharmaceutical intermediates, such as β-adrenergic blocking agents, antitumor agents, antifungal antibiotics and antidiabetic drugs. Interestingly, the nitrile hydratase-amidase system can enantioselectively hydrolyse some compounds, while the nitrilase hydrolyses the opposite enantiomer of similar nitriles [37]. Biocatalytic nitrile hydrolysis affords valuable applications in industry, including production of solvents, extractants, pharmaceuticals, drug intermediates, and pesticides [38–41].…”

Section: Introductionmentioning

confidence: 99%

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The complete genome sequence of the nitrile biocatalyst Rhodococcus rhodochrous ATCC BAA-870

Frederick

Hennessy

Horn³

et al. 2020

BMC Genomics

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BackgroundRhodococci are industrially important soil-dwelling Gram-positive bacteria that are well known for both nitrile hydrolysis and oxidative metabolism of aromatics. Rhodococcus rhodochrous ATCC BAA-870 is capable of metabolising a wide range of aliphatic and aromatic nitriles and amides. The genome of the organism was sequenced and analysed in order to better understand this whole cell biocatalyst.ResultsThe genome of R. rhodochrous ATCC BAA-870 is the first Rhodococcus genome fully sequenced using Nanopore sequencing. The circular genome contains 5.9 megabase pairs (Mbp) and includes a 0.53 Mbp linear plasmid, that together encode 7548 predicted protein sequences according to BASys annotation, and 5535 predicted protein sequences according to RAST annotation. The genome contains numerous oxidoreductases, 15 identified antibiotic and secondary metabolite gene clusters, several terpene and nonribosomal peptide synthetase clusters, as well as 6 putative clusters of unknown type. The 0.53 Mbp plasmid encodes 677 predicted genes and contains the nitrile converting gene cluster, including a nitrilase, a low molecular weight nitrile hydratase, and an enantioselective amidase.Although there are fewer biotechnologically relevant enzymes compared to those found in rhodococci with larger genomes, such as the well-known Rhodococcus jostii RHA1, the abundance of transporters in combination with the myriad of enzymes found in strain BAA-870 might make it more suitable for use in industrially relevant processes than other rhodococci.ConclusionsThe sequence and comprehensive description of the R. rhodochrous ATCC BAA-870 genome will facilitate the additional exploitation of rhodococci for biotechnological applications, as well as enable further characterisation of this model organism. The genome encodes a wide range of enzymes, many with unknown substrate specificities supporting potential applications in biotechnology, including nitrilases, nitrile hydratase, monooxygenases, cytochrome P450s, reductases, proteases, lipases, and transaminases.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The complete genome sequence of the nitrile biocatalyst Rhodococcus rhodochrous ATCC BAA-870

Frederick

Hennessy

Horn³

et al. 2020

BMC Genomics

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“…Following electrophoresis of density gradient fraction samples on precast denaturing 4–12% Bolt™ Bis-Tris Plus polyacrylamide Gels (Thermo Fischer Scientific), according to the manufacturer’s instructions, and Coomassie Brilliant Blue G250 staining and destaining, candidate protein bands of approximately the correct size were excised from the gel and sent for LCMS-MS peptide sequencing analysis, previously described by our colleagues [65]. Briefly, the protein bands were in-gel trypsin digested, resuspended in 2% acetonitrile/0.2% formic acid and analysed using a Dionex Ultimate 3000 RSLC system coupled to an AB Sciex 6600 Triple TOF mass spectrometer.…”

Section: Methodsmentioning

confidence: 99%

Plant-produced chimeric virus-like particles - a new generation vaccine against African horse sickness

et al. 2019

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BackgroundAfrican horse sickness (AHS) is a severe arthropod-borne viral disease of equids, with a mortality rate of up to 95% in susceptible naïve horses. Due to safety concerns with the current live, attenuated AHS vaccine, alternate safe and effective vaccination strategies such as virus-like particles (VLPs) are being investigated. Transient plant-based expression systems are a rapid and highly scalable means of producing such African horse sickness virus (AHSV) VLPs for vaccine purposes.ResultsIn this study, we demonstrated that transient co-expression of the four AHSV capsid proteins in agroinfiltrated Nicotiana benthamiana dXT/FT plants not only allowed for the assembly of homogenous AHSV-1 VLPs but also single, double and triple chimeric VLPs, where one capsid protein originated from one AHS serotype and at least one other capsid protein originated from another AHS serotype. Following optimisation of a large scale VLP purification procedure, the safety and immunogenicity of the plant-produced, triple chimeric AHSV-6 VLPs was confirmed in horses, the target species.ConclusionsWe have successfully shown assembly of single and double chimeric AHSV-7 VLPs, as well as triple chimeric AHSV-6 VLPs, in Nicotiana benthamiana dXT/FT plants. Plant produced chimeric AHSV-6 VLPs were found to be safe for administration into 6 month old foals as well as capable of eliciting a weak neutralizing humoral immune response in these target animals against homologous AHSV virus.

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“…R. rhodochrous nitrilase substrates include (among many others) benzonitrile for R. rhodochrous J1 [140] and crotononitrile and acrylonitrile for R. rhodochrous K22 [141]. R. rhodochrous ATCC BAA-870 expresses an enantioselective aliphatic nitrilase encoded on the plasmid, which is induced by dimethylformamide [37].…”

Section: Nitrile Conversionmentioning

confidence: 99%

mentioning

confidence: 99%

The complete genome sequence of the nitrile biocatalyst Rhodocccus rhodochrous ATCC BAA-870

Frederick

Hennessy

Horn

et al. 2019

Preprint

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Background Rhodococci are industrially important soil-dwelling Gram-positive bacteria that are well known for both nitrile hydrolysis and oxidative metabolism of aromatics. Rhodococcus rhodochrous ATCC BAA-870 is capable of metabolising a wide range of aliphatic and aromatic nitriles and amides. The genome of the organism was sequenced and analysed in order to better understand this whole cell biocatalyst. Results The genome of R. rhodochrous ATCC BAA-870 is the first Rhodococcus genome fully sequenced using Nanopore sequencing. The circular genome contains 5.9 megabase pairs (Mbp) and includes a 0.53 Mbp linear plasmid, that together encode 7548 predicted protein sequences according to BASys annotation, and 5535 predicted protein sequences according to RAST annotation. The genome contains numerous oxidoreductases, 15 identified antibiotic and secondary metabolite gene clusters, several terpene and nonribosomal peptide synthetase clusters, as well as 6 putative clusters of unknown type. The 0.53 Mbp plasmid encodes 677 predicted genes and contains the nitrile converting gene cluster, including a nitrilase, a low molecular weight nitrile hydratase, and an enantioselective amidase. Although there are fewer biotechnologically relevant enzymes compared to those found in rhodococci with larger genomes, such as the well-known Rhodococcus jostii RHA1, the abundance of transporters in combination with the myriad of enzymes found in strain BAA-870 might make it more suitable for use in industrially relevant processes than other rhodococci. Conclusions The sequence and comprehensive description of the R. rhodochrous ATCC BAA-870 genome will facilitate the additional exploitation of rhodococci for biotechnological applications, as well as enable further characterisation of this model organism. The genome encodes a wide range of enzymes, many with unknown substrate specificities supporting potential applications in biotechnology, including nitrilases, nitrile hydratase, monooxygenases, cytochrome P450s, reductases, proteases, lipases, and transaminases.

show abstract

Dimethylformamide is a novel nitrilase inducer in Rhodococcus rhodochrous

Cited by 20 publications

References 58 publications

The complete genome sequence of the nitrile biocatalyst Rhodococcus rhodochrous ATCC BAA-870

The complete genome sequence of the nitrile biocatalyst Rhodococcus rhodochrous ATCC BAA-870

Plant-produced chimeric virus-like particles - a new generation vaccine against African horse sickness

The complete genome sequence of the nitrile biocatalyst Rhodocccus rhodochrous ATCC BAA-870

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