Anfractuous assemblies of IMP dehydrogenase and CTP synthase: new twists on regulation?
| Autor: | Gregory D. McCluskey, Stephen L. Bearne |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Guanosine Biochemistry super‐resolution imaging Cell Line law.invention Protein filament 03 medical and health sciences chemistry.chemical_compound IMP Dehydrogenase IMP dehydrogenase Confocal microscopy law Carbon-Nitrogen Ligases heterocyclic compounds Nucleotide Molecular Biology CTP synthase chemistry.chemical_classification live‐cell imaging Nucleotides cytoophidium Original Articles Cell Biology Fusion protein enzymes and coenzymes (carbohydrates) 030104 developmental biology chemistry Cell culture Original Article Function (biology) |
| Zdroj: | The Febs Journal |
| ISSN: | 1742-4658 1742-464X |
| DOI: | 10.1111/febs.14658 |
| Popis: | Inosine monophosphate dehydrogenase (IMPDH) and cytidine triphosphate synthase (CTPS) are two metabolic enzymes that perform rate‐limiting steps in the de novo synthesis of purine and pyrimidine nucleotides, respectively. It has been shown that IMPDH and CTPS can comprise a filamentous macrostructure termed the cytoophidium, which may play a role in regulation of their catalytic activity. Although these two proteins may colocalise in the same cytoophidium, how they associate with one another is still elusive. As reported herein, we established a model HeLa cell line coexpressing OFP‐tagged IMPDH2 and GFP‐tagged CTPS1 and recorded the assembly, disassembly and movement of the cytoophidium in live cells. Moreover, by using super‐resolution confocal imaging, we demonstrate how IMPDH‐ and CTPS‐based filaments are aligned or intertwined in the mixed cytoophidium. Collectively, our findings provide a panorama of cytoophidium dynamics and suggest that IMPDH and CTPS cytoophidia may coordinate by interfilament interaction. |
| Databáze: | OpenAIRE |
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