A Lanthipeptide-like N-Terminal Leader Region Guides Peptide Epimerization by Radical SAM Epimerases: Implications for RiPP Evolution

详细信息    查看全文

• 作者：Dr. Sebastian W. Fuchs ; Dr. Gerald Lackner ; Dr. Brandon I. Morinaka ; Yohei Morishita ; Prof. Dr. Teigo Asai ; Prof. Sereina Riniker and Prof. Dr. Jö ; rn Piel
• 刊名：Angewandte Chemie
• 出版年：2016
• 出版时间：September 26, 2016
• 年：2016
• 卷：128
• 期：40
• 页码：12518-12521
• 全文大小：1772K
• ISSN：1521-3757

文摘

Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the prototype members polytheonamides being generated by almost 50 maturation steps, including introduction of d-residues at multiple positions by an unusual radical SAM epimerase. A region in the protein-like N-terminal leader of proteusin precursors is identified that is crucial for epimerization. It resembles a precursor motif previously shown to mediate interaction in thioether bridge-formation in class I lanthipeptide biosynthesis. Beyond this region, similarities were identified between proteusin and further RiPP families, including class I lanthipeptides. The data suggest that common leader features guide distinct maturation types and that nitrile hydratase-like enzymes are ancestors of several RiPP classes.