Fengycin, a lipopeptidic antibiotic, is synthesized nonribosomally by five fengycin synthetases (FenC, FenD, FenE, FenA, and FenB) in Bacillus subtilis F29-3. This work demonstrates that these fengycin synthetases interlock to form a chain, which coils into a 14.5-nm structure. In this chain, fengycin synthetases are linked in the order FenC-FenD-FenE-FenA-FenB by interactions between the C-ter...

Microorganisms produce a large number of pharmacologically and biotechnologically important peptides by using nonribosomal peptide synthetases (NRPSs). Due to their modular arrangement and their domain organization NRPSs are particularly suitable for engineering recombinant proteins for the production of novel peptides with interesting properties. In order to compare different strategies of dom...

Accuracy of protein synthesis is critical for life since a high degree of fidelity of the translation of the genetic information is required to accomplish the needs of the cellular functions as well as to preserve the variability developed by evolution. More than one hundred macromolecules are involved in this process even in the simplest organisms, including ribosomal proteins, translation fac...

The rapid emergence of antimicrobial resistance in clinical settings has called for renewed efforts to discover and develop new compounds. Lanthipeptides present a promising, genetically encoded molecular scaffold the engineering structurally complex, biologically active peptides. These peptide natural products are constructed by enzymes (lanthipeptide synthetases) with relaxed substrate specif...

Cytoplasmic aminoacyl-tRNA synthetases of higher eukaryotes acquired extra peptides in the course of their evolution. It has been thought that these appendices are related to the occurrence of the multiprotein complex consisting of at least eight different tRNA synthetase polypeptides. This complex is believed to be a signature feature of metazoans. In this study, we used multiple sequence alig...