Discovery of Thanafactin A, a Linear, Proline-Containing Octalipopeptide from Pseudomonas sp. SH-C52, Motivated by Genome Mining

Norbert Kirchner, Carolina Cano-Prieto, Anna Christina Schulz-Fincke, Michael Gütschow, Nico Ortlieb, Julia Moschny, Timo H.J. Niedermeyer, Jeannie Horak, Michael Lämmerhofer, Menno Van Der Voort, Jos M. Raaijmakers, Harald Gross*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

1 Citation (Scopus)

Abstract

Genome mining of the bacterial strains Pseudomonas sp. SH-C52 and Pseudomonas fluorescens DSM 11579 showed that both strains contained a highly similar gene cluster encoding an octamodular nonribosomal peptide synthetase (NRPS) system which was not associated with a known secondary metabolite. Insertional mutagenesis of an NRPS component followed by comparative profiling led to the discovery of the corresponding novel linear octalipopeptide thanafactin A, which was subsequently isolated and its structure determined by two-dimensional NMR and further spectroscopic and chromatographic methods. In bioassays, thanafactin A exhibited weak protease inhibitory activity and was found to modulate swarming motility in a strain-specific manner.

Original languageEnglish
Pages (from-to)101-109
Number of pages9
JournalJournal of Natural Products
Volume84
Issue number1
DOIs
Publication statusPublished - 31 Dec 2020

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