Enzymatic synthesis of bioinformatically predicted microcin C-like compounds encoded by diverse bacteria

Olga Bantysh, Marina Serebryakova, Kira S. Makarova, Svetlana Dubiley, Kirill A. Datsenko, Konstantin Severinov

    Research output: Contribution to journalArticlepeer-review

    23 Citations (Scopus)

    Abstract

    The Trojan horse Escherichia coli antibiotic microcin C (McC) consists of a heptapeptide attached to adenosine through a phosphoramidate linkage. McC is synthesized by the MccB enzyme, which terminally adenylates the ribosomally synthesized heptapeptide precursor MccA. The peptide part is responsible for McC uptake; it is degraded inside the cell to release a toxic nonhydrolyzable aspartyl-adenylate. Bionformatic analysis reveals that diverse bacterial genomes encoding mccB homologues also contain adjacent short open reading frames that may encode MccA-like adenylation substrates. Using chemically synthesized predicted peptide substrates and recombinant cognate MccB protein homologs, adenylated products were obtained in vitro for predicted MccA peptide-MccB enzyme pairs from Helicobacter pylori, Streptococcus thermophilus, Lactococcus johnsonii, Bartonella washoensis, Yersinia pseudotuberculosis, and Synechococcus sp. Some adenylated products were shown to inhibit the growth of E. coli by targeting aspartyl-tRNA synthetase, the target of McC.

    Original languageEnglish
    Article numbere01059-14
    JournalmBio
    Volume5
    Issue number3
    DOIs
    Publication statusPublished - 6 May 2014

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