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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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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. |
format | Online Article Text |
id | pubmed-4542470 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
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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