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

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...

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Autores principales: Karagianni, Eleni P., Kontomina, Evanthia, Davis, Britton, Kotseli, Barbara, Tsirka, Theodora, Garefalaki, Vasiliki, Sim, Edith, Glenn, Anthony E., Boukouvala, Sotiria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542470/
https://www.ncbi.nlm.nih.gov/pubmed/26245863
http://dx.doi.org/10.1038/srep12900
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author Karagianni, Eleni P.
Kontomina, Evanthia
Davis, Britton
Kotseli, Barbara
Tsirka, Theodora
Garefalaki, Vasiliki
Sim, Edith
Glenn, Anthony E.
Boukouvala, Sotiria
author_facet Karagianni, Eleni P.
Kontomina, Evanthia
Davis, Britton
Kotseli, Barbara
Tsirka, Theodora
Garefalaki, Vasiliki
Sim, Edith
Glenn, Anthony E.
Boukouvala, Sotiria
author_sort Karagianni, Eleni P.
collection PubMed
description 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.
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spelling pubmed-45424702015-09-01 Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family Karagianni, Eleni P. Kontomina, Evanthia Davis, Britton Kotseli, Barbara Tsirka, Theodora Garefalaki, Vasiliki Sim, Edith Glenn, Anthony E. Boukouvala, Sotiria Sci Rep Article 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. Nature Publishing Group 2015-08-06 /pmc/articles/PMC4542470/ /pubmed/26245863 http://dx.doi.org/10.1038/srep12900 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Karagianni, Eleni P.
Kontomina, Evanthia
Davis, Britton
Kotseli, Barbara
Tsirka, Theodora
Garefalaki, Vasiliki
Sim, Edith
Glenn, Anthony E.
Boukouvala, Sotiria
Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family
title Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family
title_full Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family
title_fullStr Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family
title_full_unstemmed Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family
title_short Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family
title_sort homologues of xenobiotic metabolizing n-acetyltransferases in plant-associated fungi: novel functions for an old enzyme family
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542470/
https://www.ncbi.nlm.nih.gov/pubmed/26245863
http://dx.doi.org/10.1038/srep12900
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