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Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Liao, Rijing Duan, Lian Lei, Chun Kwok Pan, Haixue Ding, Ying Zhang, Qi Chen, Daijie Shen, Ben |
| Copyright Year | 2009 |
| Abstract | Thiopeptides, with potent activity against various drug-resistant pathogens, contain a characteristic macrocyclic core consisting of multiple thiazoles, dehydroamino acids, and a 6-membered nitrogen heterocycle. Their biosynthetic pathways remain elusive, in spite of great efforts by in vivo feeding experiments. Here, cloning, sequencing, and characterization of the thiostrepton and siomycin A gene clusters unveiled a biosynthetic paradigm for the thiopeptide specific core formation, featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications. The paradigm generality for thiopeptide biosynthesis was supported by genome mining and ultimate confirmation of the thiocillin I production in Bacillus cereus ATCC 14579, a strain that was previously unknown as a thiopeptide producer. These findings set the stage to accelerate the discovery of thiopeptides by prediction at the genetic level and to generate structural diversity by applying combinatorial biosynthesis methods. |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/j.chembiol.2009.01.007 |
| PubMed reference number | 19246004 |
| Journal | Medline |
| Volume Number | 16 |
| Issue Number | 2 |
| Alternate Webpage(s) | http://www.cell.com/cms/attachment/604978/4798375/mmc1.pdf |
| Alternate Webpage(s) | http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2676563&blobtype=pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/j.chembiol.2009.01.007 |
| Journal | Chemistry & biology |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
