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Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibition
Skolkovo Inst Sci & Technol, Ctr Life Sci, Moscow, Russia;Russian Acad Sci, Inst Gene Biol, Moscow, Russia.
Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Systems Biology. Skolkovo Inst Sci & Technol, Ctr Life Sci, Moscow, Russia;Russian Acad Sci, Inst Gene Biol, Moscow, Russia.ORCID iD: 0000-0003-2829-6395
Univ Calif Berkeley, Dept Mol & Cell Biol, 229 Stanley Hall, Berkeley, CA 94720 USA.
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2019 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, article id 4563Article in journal (Refereed) Published
Abstract [en]

Ribosome-synthesized post-translationally modified peptides (RiPPs) represent a rapidly expanding class of natural products with various biological activities. Linear azol(in)e-containing peptides (LAPs) comprise a subclass of RiPPs that display outstanding diversity of mechanisms of action while sharing common structural features. Here, we report the discovery of a new LAP biosynthetic gene cluster in the genome of Rhizobium Pop5, which encodes the precursor peptide and modification machinery of phazolicin (PHZ) - an extensively modified peptide exhibiting narrow-spectrum antibacterial activity against some symbiotic bacteria of leguminous plants. The cryo-EM structure of the Escherichia coli 70S-PHZ complex reveals that the drug interacts with the 23S rRNA and uL4/uL22 proteins and obstructs ribosomal exit tunnel in a way that is distinct from other compounds. We show that the uL4 loop sequence determines the species-specificity of antibiotic action. PHZ expands the known diversity of LAPs and may be used in the future as biocontrol agent for agricultural needs.

Place, publisher, year, edition, pages
Nature Publishing Group, 2019. Vol. 10, article id 4563
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-396722DOI: 10.1038/s41467-019-12589-5ISI: 000489101100007PubMedID: 31594941OAI: oai:DiVA.org:uu-396722DiVA, id: diva2:1375952
Funder
NIH (National Institute of Health), R01-GM132302NIH (National Institute of Health), R21AI137584NIH (National Institute of Health), R01-GM114454Available from: 2019-12-06 Created: 2019-12-06 Last updated: 2019-12-12Bibliographically approved

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