Biosynthetic Studies of Phomopsins Unveil Posttranslational Installation of Dehydroamino Acids by UstYa Family Proteins

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  • Kaho Sogahata
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan
  • Taro Ozaki
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan
  • Yuya Igarashi
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan
  • Yuka Naganuma
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan
  • Chengwei Liu
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan
  • Atsushi Minami
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan
  • Hideaki Oikawa
    Department of Chemistry Faculty of Science Hokkaido University Sapporo 060-0810 Japan

抄録

<jats:title>Abstract</jats:title><jats:p>UstYa family proteins (DUF3328) are widely and specifically distributed in fungi. They are known to be involved in the biosynthesis of ribosomally synthesized and posttranslationally modified peptides (RiPPs) and nonribosomal peptides, and possibly catalyze various reactions, including oxidative cyclization and chlorination. In this study, we focused on phomopsin A, a fungal RiPP consisting of unique nonproteinogenic amino acids. Gene knockout experiments demonstrated that three UstYa homologues, <jats:italic>phomYc</jats:italic>, <jats:italic>phomYd</jats:italic>, and <jats:italic>phomYe</jats:italic>, are essential for the desaturation of amino acid moieties, showing unprecedented function among UstYa family proteins. Sequence similarity network analysis indicated that their amino acid sequences are highly diverged and that most remain uncharacterized, paving the way for genome mining of fungal metabolites with unique modifications.</jats:p>

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