Journal
CHEMISTRY & BIOLOGY
Volume 21, Issue 6, Pages 766-774Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2014.04.008
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Funding
- PRESTO
- Japan Science and Technology Agency (JST)
- Japan Society for the Promotion of Science [22750145]
- Daiichi-Sankyo Foundation of Life Science
- JSPS [21000005]
- CREST, JST
- Grants-in-Aid for Scientific Research [21000005, 22750145] Funding Source: KAKEN
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Azoline moieties in the backbones of peptidic natural products are important structural motifs that contribute to diverse bioactivities. Some azoline-containing peptides (Az-peptides) are produced from ribosomally synthesized precursor peptides, in which cysteine, serine, and threonine residues are converted to their corresponding azolines by post-translational modification through a cyclodehydratase. We have devised an in vitro biosynthesis system of Az-peptides, referred to as the FIT-PatD (flexible in vitro translation) system, by the integration of a cell-free translation system with the post-translational cyclodehydratase PatD. This system enabled the one-pot'' synthesis of a wide variety of Az-peptide derivatives expressed from synthetic DNA templates. The FIT-PatD system also facilitated mutagenesis studies on a wide array of precursor peptide sequences, unveiling unique in vitro substrate tolerance of PatD.
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