Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Gene Expression
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Genetic Complementation Test
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Lichens / classification
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Lichens / enzymology*
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Lichens / genetics*
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Molecular Sequence Data
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Piperidones / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Sequence Alignment
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Transferases (Other Substituted Phosphate Groups) / chemistry
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Transferases (Other Substituted Phosphate Groups) / genetics*
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Transferases (Other Substituted Phosphate Groups) / metabolism*
Substances
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Bacterial Proteins
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Fungal Proteins
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Piperidones
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phosphopantetheinyl transferase
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indigoidine
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Transferases (Other Substituted Phosphate Groups)
Grants and funding
This work was supported by the Hessian Ministry of Science and Art via the LOEWE research focus "Integrative fungal research (IPF)".