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Efficient in vivo synthesis of lasso peptide pseudomycoidin proceeds in the absence of both the leader and the leader peptidase
Skolkovo Inst Sci & Technol, Ctr Life Sci, Moscow, Russia; Peter Great St Petersburg Polytech Univ, St Petersburg, Russia.
Skolkovo Inst Sci & Technol, Ctr Life Sci, Moscow, Russia; Lomonosov Moscow State Univ, AN Belozersky Inst Physicochem Biol, Moscow Russia; Russian Acad Sci, Inst Gene Biol, Moscow, Russia.
Skolkovo Inst Sci & Technol, Moscow, Russia; Russian Acad Sci, Moscow, Russia.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Systems Biology. Skolkovo Inst Sci & Technol, Moscow, Russia; Peter Great St Petersburg Polytech Univ, St Petersburg, Russia; Russian Acad Sci, Inst Gene Biol, Moscow Russia.ORCID iD: 0000-0003-2829-6395
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2019 (English)In: Chemical Science, ISSN 2041-6520, E-ISSN 2041-6539, Vol. 10, no 42, p. 9699-9707Article in journal (Refereed) Published
Abstract [en]

Bacterial lasso peptides are made from linear ribosomally synthesized precursors by specific cleavage at the leader-core junction site of the precursor by a dedicated protease recognizing the leader, followed by cyclisation of the newly formed N-terminus of the core part with a side chain of the internal aspartic or glutamic residue catalyzed by a macrolactam synthetase. The resulting structure has a tail that is threaded and fixed inside the cycle formed. Here, we characterize a new lasso peptide, pseudomycoidin, encoded by Bacillus pseudomycoides DSM 12442. The most surprising and unique feature of pseudomycoidin is that it can be produced in vivo from the ribosomally synthesized core part by a macrolactam synthetase, in the absence of the leader protease. The minimalism of the pseudomycoidin synthesis system makes it a powerful model to generate pseudomycoidin-based lasso-peptide libraries and to study the poorly understood process of lasso formation. We detected two additional pseudomycoidin modifications: phosphorylation of a terminal residue that was previously observed in another lasso peptide, followed by glycosylation, which was not observed heretofore. We speculate that these bulky C-terminal modifications may help maintain the threaded lasso topology of the compound synthesized by the macrolactam synthetase.

Place, publisher, year, edition, pages
2019. Vol. 10, no 42, p. 9699-9707
National Category
Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-397636DOI: 10.1039/c9sc02370dISI: 000493521200006OAI: oai:DiVA.org:uu-397636DiVA, id: diva2:1372259
Funder
European Regional Development Fund (ERDF)Available from: 2019-11-22 Created: 2019-11-22 Last updated: 2019-11-22Bibliographically approved

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