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Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri

In the last decades, natural products from lichens have gained more interest for pharmaceutical application due to the broad range of their biological activity. However, isolation of the compounds of interest directly from the lichen is neither feasible nor sustainable due to slow growth of many lic...

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Detalles Bibliográficos
Autores principales: Schimming, Olivia, Schmitt, Imke, Bode, Helge B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4718654/
https://www.ncbi.nlm.nih.gov/pubmed/26784935
http://dx.doi.org/10.1371/journal.pone.0145624
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author Schimming, Olivia
Schmitt, Imke
Bode, Helge B.
author_facet Schimming, Olivia
Schmitt, Imke
Bode, Helge B.
author_sort Schimming, Olivia
collection PubMed
description In the last decades, natural products from lichens have gained more interest for pharmaceutical application due to the broad range of their biological activity. However, isolation of the compounds of interest directly from the lichen is neither feasible nor sustainable due to slow growth of many lichens. In order to develop a pipeline for heterologous expression of lichen biosynthesis gene clusters and thus the sustainable production of their bioactive compounds we have identified and characterized the phosphopantheteinyl transferase (PPTase) EppA from the lichen Evernia prunastri. The Sfp-type PPTase EppA was functionally characterized through heterologous expression in E. coli using the production of the blue pigment indigoidine as readout and by complementation of a lys5 deletion in S. cerevisiae.
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spelling pubmed-47186542016-01-30 Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri Schimming, Olivia Schmitt, Imke Bode, Helge B. PLoS One Research Article In the last decades, natural products from lichens have gained more interest for pharmaceutical application due to the broad range of their biological activity. However, isolation of the compounds of interest directly from the lichen is neither feasible nor sustainable due to slow growth of many lichens. In order to develop a pipeline for heterologous expression of lichen biosynthesis gene clusters and thus the sustainable production of their bioactive compounds we have identified and characterized the phosphopantheteinyl transferase (PPTase) EppA from the lichen Evernia prunastri. The Sfp-type PPTase EppA was functionally characterized through heterologous expression in E. coli using the production of the blue pigment indigoidine as readout and by complementation of a lys5 deletion in S. cerevisiae. Public Library of Science 2016-01-19 /pmc/articles/PMC4718654/ /pubmed/26784935 http://dx.doi.org/10.1371/journal.pone.0145624 Text en © 2016 Schimming et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Schimming, Olivia
Schmitt, Imke
Bode, Helge B.
Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri
title Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri
title_full Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri
title_fullStr Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri
title_full_unstemmed Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri
title_short Identification of the Sfp-Type PPTase EppA from the Lichenized Fungus Evernia prunastri
title_sort identification of the sfp-type pptase eppa from the lichenized fungus evernia prunastri
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4718654/
https://www.ncbi.nlm.nih.gov/pubmed/26784935
http://dx.doi.org/10.1371/journal.pone.0145624
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