Peter Grün

TL;DR: A new mechanism for the cleavage and activation of nonribosomally made peptides and peptide-polyketide hybrids that are apparently operational in several different bacteria is identified.

TL;DR: Comparative genomics and high-resolution mass spectrometry reveal the biosynthetic gene clusters, and vast chemical diversity of natural products that they encode, in Photorhabdus and XenorhabDus, bacteria that interact with hosts as symbionts and entomopathogens.

TL;DR: A new fusion point inside the condensation domains of NRPSs is described that results in the development of the exchange unit condensation domain (XUC) concept, which enables the efficient production of peptides, even containing non-natural amino acids, in yields up to 280 mg l−1.

TL;DR: A combination of stable isotope labeling of Photorhabdus and XenorhabDus strains and their transaminase mutants followed by detailed MS analysis enabled the structure elucidation of novel cyclopeptides named GameXPeptides including their absolute configuration in crude extracts without their actual isolation.

TL;DR: The gene cluster encoding the fimsbactin synthetase (fbs) was identified in both genomes, and mutants in fbs genes in A. baylyi were analyzed, thus allowing prediction of the fimbactin biosynthesis pathway.