ArticleScientific reports2019
Saccharomyces cerevisiae ASN1 and ASN2 are asparagine synthetase paralogs that have diverged in their ability to polymerize in response to nutrient stress.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026Review
- Imaging Techniques for the Study of Protein Condensates and Filaments and Their Applications.International journal of molecular sciences · 2026Review
- Article
- Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.G3 (Bethesda, Md.) · 2021Article
- Reduced free asparagine in wheat grain resulting from a natural deletion of TaASN-B2: investigating and exploiting diversity in the asparagine synthetase gene family to improve wheat quality.BMC plant biology · 2021Article
- Phosphofructokinase relocalizes into subcellular compartments with liquid-like properties in vivo.Biophysical journal · 2021Article
- Effects of A6E Mutation on Protein Expression and Supramolecular Assembly of Yeast Asparagine Synthetase.Biology · 2021Article
- ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2021Article
- Coupled regulations of enzymatic activity and structure formation of aldehyde dehydrogenase Ald4p.Biology open · 2020Article
- Article
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
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3 authors.
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Abstract
Recent work has found that many metabolic enzymes have the ability to polymerize in response to metabolic changes or environmental stress. This ability to polymerize is well conserved for the few metabolic enzyme paralogs that have been studied in yeast. Here we describe the first set of paralogs, Asn1p and Asn2p, that have differential assembly behavior. Asn1p and Asn2p both co-assemble into filaments in response to nutrient limitation. However, the ability of Asn2p to form filaments is strictly dependent on the presence of Asn1p. Using mutations that block enzyme activity but have differential effects on Asn1p polymerization, we have found that Asn1p polymers are unlikely to have acquired a moonlighting function. Together these results provide a novel system for understanding the regulation and evolution of metabolic enzyme polymerization.
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