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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/87349

Title: Biosynthetic Studies of Phomopsins Unveil Posttranslational Installation of Dehydroamino Acids by UstYa Family Proteins
Authors: Sogahata, Kaho Browse this author
Ozaki, Taro Browse this author
Igarashi, Yuya Browse this author
Naganuma, Yuka Browse this author
Liu, Chengwei Browse this author
Minami, Atsushi Browse this author
Oikawa, Hideaki Browse this author →KAKEN DB
Keywords: biosynthesis
enzymes
halogenation
natural products
peptides
Issue Date: 1-Dec-2021
Publisher: Wiley-Blackwell
Journal Title: Angewandte chemie-international edition
Volume: 60
Issue: 49
Start Page: 25729
End Page: 25734
Publisher DOI: 10.1002/anie.202111076
Abstract: 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, phomYc, phomYd, and phomYe, 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.
Rights: This is the peer reviewed version of the following article: Angewandte Chemie International Edition 60(49) pp.25729-25734, which has been published in final form at https://doi.org/10.1002/anie.202111076. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
Type: article (author version)
URI: http://hdl.handle.net/2115/87349
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 及川 英秋

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