Publication: A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network
Issued Date
2019-10-01
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ISSN
19394586
10591524
10591524
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2-s2.0-85072792078
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Mahidol University
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SCOPUS
Bibliographic Citation
Molecular Biology of the Cell. Vol.30, No.21 (2019), 2721-2736
Suggested Citation
Chalongrat Noree, Kyle Begovich, Dane Samilo, Risa Broyer, Elena Monfort, James E. Wilhelm A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network. Molecular Biology of the Cell. Vol.30, No.21 (2019), 2721-2736. doi:10.1091/mbc.E19-04-0224 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/50067
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Title
A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network
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Abstract
© 2019 Noree et al. Despite the proliferation of proteins that can form filaments or phase-separated condensates, it remains unclear how this behavior is distributed over biological networks. We have found that 60 of the 440 yeast metabolic enzymes robustly form structures, including 10 that assemble within mitochondria. Additionally, the ability to assemble is enriched at branch points on several metabolic pathways. The assembly of enzymes at the first branch point in de novo purine biosynthesis is coordinated, hierarchical, and based on their position within the pathway, while the enzymes at the second branch point are recruited to RNA stress granules. Consistent with distinct classes of structures being deployed at different control points in a pathway, we find that the first enzyme in the pathway, PRPP synthetase, forms evolutionarily conserved filaments that are sequestered in the nucleus in higher eukaryotes. These findings provide a roadmap for identifying additional conserved features of metabolic regulation by condensates/filaments.