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Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family.

Karagianni EP, Kontomina E, Davis B, Kotseli B, Tsirka T, Garefalaki V, Sim E, Glenn AE, Boukouvala S - Sci Rep (2015)

Bottom Line: Plant-pathogenic fungi and their hosts engage in chemical warfare, attacking each other with toxic products of secondary metabolism and defending themselves via an arsenal of xenobiotic metabolizing enzymes.The third group generates minimal activity with acyl-CoA compounds that bind non-selectively to the proteins.We propose that fungal NAT isoenzymes may have evolved to perform diverse functions, potentially relevant to pathogen fitness, acetyl-CoA/propionyl-CoA intracellular balance and secondary metabolism.

View Article: PubMed Central - PubMed

Affiliation: Democritus University of Thrace, Department of Molecular Biology and Genetics, Alexandroupolis 68100, Greece.

ABSTRACT
Plant-pathogenic fungi and their hosts engage in chemical warfare, attacking each other with toxic products of secondary metabolism and defending themselves via an arsenal of xenobiotic metabolizing enzymes. One such enzyme is homologous to arylamine N-acetyltransferase (NAT) and has been identified in Fusarium infecting cereal plants as responsible for detoxification of host defence compound 2-benzoxazolinone. Here we investigate functional diversification of NAT enzymes in crop-compromising species of Fusarium and Aspergillus, identifying three groups of homologues: Isoenzymes of the first group are found in all species and catalyse reactions with acetyl-CoA or propionyl-CoA. The second group is restricted to the plant pathogens and is active with malonyl-CoA in Fusarium species infecting cereals. The third group generates minimal activity with acyl-CoA compounds that bind non-selectively to the proteins. We propose that fungal NAT isoenzymes may have evolved to perform diverse functions, potentially relevant to pathogen fitness, acetyl-CoA/propionyl-CoA intracellular balance and secondary metabolism.

No MeSH data available.


Related in: MedlinePlus

Fungal tolerance of 2-benzoxazolinone.F. verticillioides (G. moniliformis) strain FGSC 7600 (a), F. graminearum (G. zeae) strain PH-1 (b), F. oxysporum f.sp. lycopersici strain FOL 4287 (c),A. flavus strain NRRL 3357 (d) and A. nidulans (E. nidulans) strain FGSC A4 (e) were grown on standard agar medium supplemented with up to 1000 μg/ml of 2-benzoxazolinone. Cultures are shown after 5 days of incubation.
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f5: Fungal tolerance of 2-benzoxazolinone.F. verticillioides (G. moniliformis) strain FGSC 7600 (a), F. graminearum (G. zeae) strain PH-1 (b), F. oxysporum f.sp. lycopersici strain FOL 4287 (c),A. flavus strain NRRL 3357 (d) and A. nidulans (E. nidulans) strain FGSC A4 (e) were grown on standard agar medium supplemented with up to 1000 μg/ml of 2-benzoxazolinone. Cultures are shown after 5 days of incubation.

Mentions: The results of the enzymatic assays measuring endogenous N-malonyltransferase activity are reflected in the ability of the ascomycetes to tolerate BOA in solid culture media. F. verticillioides grew effectively on media with up to 1 mg/ml BOA, a toxic concentration for other fungi. F. graminearum also tolerated BOA, but radial growth was slower and toxicity was evident at 1 mg/ml concentration of the compound. F. oxysporum and A. flavus, on the other hand, were sensitive to BOA, with delayed growth evident on media with lower concentrations of the compound. Consistent with our observations above, growth of N-malonyltransferase deficient A. nidulans was much reduced at the lowest concentration of BOA, and the higher concentrations completely inhibited growth (Fig. 5).


Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family.

Karagianni EP, Kontomina E, Davis B, Kotseli B, Tsirka T, Garefalaki V, Sim E, Glenn AE, Boukouvala S - Sci Rep (2015)

Fungal tolerance of 2-benzoxazolinone.F. verticillioides (G. moniliformis) strain FGSC 7600 (a), F. graminearum (G. zeae) strain PH-1 (b), F. oxysporum f.sp. lycopersici strain FOL 4287 (c),A. flavus strain NRRL 3357 (d) and A. nidulans (E. nidulans) strain FGSC A4 (e) were grown on standard agar medium supplemented with up to 1000 μg/ml of 2-benzoxazolinone. Cultures are shown after 5 days of incubation.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4542470&req=5

f5: Fungal tolerance of 2-benzoxazolinone.F. verticillioides (G. moniliformis) strain FGSC 7600 (a), F. graminearum (G. zeae) strain PH-1 (b), F. oxysporum f.sp. lycopersici strain FOL 4287 (c),A. flavus strain NRRL 3357 (d) and A. nidulans (E. nidulans) strain FGSC A4 (e) were grown on standard agar medium supplemented with up to 1000 μg/ml of 2-benzoxazolinone. Cultures are shown after 5 days of incubation.
Mentions: The results of the enzymatic assays measuring endogenous N-malonyltransferase activity are reflected in the ability of the ascomycetes to tolerate BOA in solid culture media. F. verticillioides grew effectively on media with up to 1 mg/ml BOA, a toxic concentration for other fungi. F. graminearum also tolerated BOA, but radial growth was slower and toxicity was evident at 1 mg/ml concentration of the compound. F. oxysporum and A. flavus, on the other hand, were sensitive to BOA, with delayed growth evident on media with lower concentrations of the compound. Consistent with our observations above, growth of N-malonyltransferase deficient A. nidulans was much reduced at the lowest concentration of BOA, and the higher concentrations completely inhibited growth (Fig. 5).

Bottom Line: Plant-pathogenic fungi and their hosts engage in chemical warfare, attacking each other with toxic products of secondary metabolism and defending themselves via an arsenal of xenobiotic metabolizing enzymes.The third group generates minimal activity with acyl-CoA compounds that bind non-selectively to the proteins.We propose that fungal NAT isoenzymes may have evolved to perform diverse functions, potentially relevant to pathogen fitness, acetyl-CoA/propionyl-CoA intracellular balance and secondary metabolism.

View Article: PubMed Central - PubMed

Affiliation: Democritus University of Thrace, Department of Molecular Biology and Genetics, Alexandroupolis 68100, Greece.

ABSTRACT
Plant-pathogenic fungi and their hosts engage in chemical warfare, attacking each other with toxic products of secondary metabolism and defending themselves via an arsenal of xenobiotic metabolizing enzymes. One such enzyme is homologous to arylamine N-acetyltransferase (NAT) and has been identified in Fusarium infecting cereal plants as responsible for detoxification of host defence compound 2-benzoxazolinone. Here we investigate functional diversification of NAT enzymes in crop-compromising species of Fusarium and Aspergillus, identifying three groups of homologues: Isoenzymes of the first group are found in all species and catalyse reactions with acetyl-CoA or propionyl-CoA. The second group is restricted to the plant pathogens and is active with malonyl-CoA in Fusarium species infecting cereals. The third group generates minimal activity with acyl-CoA compounds that bind non-selectively to the proteins. We propose that fungal NAT isoenzymes may have evolved to perform diverse functions, potentially relevant to pathogen fitness, acetyl-CoA/propionyl-CoA intracellular balance and secondary metabolism.

No MeSH data available.


Related in: MedlinePlus