ArticlePLoS biology2025
Phase separation of the PRPP amidotransferase into dynamic condensates promotes de novo purine synthesis in yeast.
Article in PLoS biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Transcriptomics reveals metabolic division of labor and reproduction-metabolism decoupling iniScience · 2026Article
- Integrated Transcriptomic and Metabolomic Analyses Reveal Acyl-CoA Dehydrogenase-Mediated Primordium Formation and Metabolite Synthesis inJournal of fungi (Basel, Switzerland) · 2026Article
- Mitochondrial protein import stress causes lysosomal damage and progressive tissue atrophy.EMBO reports · 2026Article
- NUDT5 regulates purine metabolism and thiopurine sensitivity by interacting with PPAT.Science (New York, N.Y.) · 2025Article
- Phase Separation-Regulated Fungal Growth, Sexual Development, Adaptation and Synthetic Biology Applications.Journal of fungi (Basel, Switzerland) · 2025Review
- In vitro Condensation Assay of Fluorescent Protein-Fused PRPP Amidotransferase Purified from Budding Yeast Cells.Bio-protocol · 2025Article
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Authors and funding
4 authors.
Funding
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Abstract
De novo purine synthesis (DPS) is up-regulated under conditions of high purine demand to ensure the production of genetic materials and chemical energy, thereby supporting cell proliferation. However, the regulatory mechanisms governing DPS remain unclear. We herein show that PRPP amidotransferase (PPAT), the rate-limiting enzyme in DPS, forms dynamic and motile condensates in Saccharomyces cerevisiae cells under a purine-depleted environment. The formation and maintenance of condensates requires phase separation, which is driven by target of rapamycin complex 1 (TORC1)-induced ribosome biosynthesis. The self-assembly of PPAT molecules facilitates condensate formation, with intracellular PRPP and purine nucleotides both regulating this self-assembly. Moreover, molecular dynamics simulations suggest that clustering-mediated PPAT activation occurs through intermolecular substrate channeling. Cells unable to form PPAT condensates exhibit growth defects, highlighting the physiological importance of condensation. These results indicate that PPAT condensation is an adaptive mechanism that regulates DPS in response to both TORC1 activity and cellular purine demands.
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