ArticleBiochemistry2025
Cysimiditides: RiPPs with a Zn-Tetracysteine Motif and Aspartimidylation.
Article in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron Oxidative Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron-Dependent Oxidative Enzyme during RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Aspartimide Modification in RiPP Natural Products.Biochemistry · 2026Review
- AlphaFold3: An Overview of Applications and Performance Insights.International journal of molecular sciences · 2025Review
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Authors and funding
4 authors.
Funding
Abstract
Aspartimidylation is a post-translational modification found in multiple families of ribosomally synthesized and post-translationally modified peptides (RiPPs). We recently reported on the imiditides, a new RiPP family in which aspartimidylation is the class-defining modification. Imiditide biosynthetic gene clusters encode a precursor protein and a methyltransferase that methylates a specific Asp residue, converting it to aspartimide. A subset of imiditides harbor a tetracysteine motif, so we have named these molecules cysimiditides. Here, using genome mining, we show that there are 56 putative cysimiditides predicted in publicly available genome sequences, all within actinomycetota. We successfully heterologously expressed two examples of cysimiditides and showed that the major products are aspartimidylated and that the tetracysteine motif is necessary for protein stability. Cysimiditides bind a Zn
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