The proline synthesis enzyme P5CS forms cytoophidia in Drosophila.
J Genet Genomics
; 47(3): 131-143, 2020 03 20.
Article
en En
| MEDLINE
| ID: mdl-32317150
ABSTRACT
Compartmentation of enzymes via filamentation has arisen as a mechanism for the regulation of metabolism. In 2010, three groups independently reported that CTP synthase (CTPS) can assemble into a filamentous structure termed the cytoophidium. In searching for CTPS-interacting proteins, here we perform a yeast two-hybrid screening of Drosophila proteins and identify a putative CTPS-interacting protein, â³1-pyrroline-5-carboxylate synthase (P5CS). Using the Drosophila follicle cell as the in vivo model, we confirm that P5CS forms cytoophidia, which are associated with CTPS cytoophidia. Overexpression of P5CS increases the length of CTPS cytoophidia. Conversely, filamentation of CTPS affects the morphology of P5CS cytoophidia. Finally, in vitro analyses confirm the filament-forming property of P5CS. Our work links CTPS with P5CS, two enzymes involved in the rate-limiting steps in pyrimidine and proline biosynthesis, respectively.
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Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Ornitina-Oxo-Ácido Transaminasa
/
Citoesqueleto
/
Prolina
/
Ligasas de Carbono-Nitrógeno
Idioma:
En
Revista:
J Genet Genomics
Año:
2020
Tipo del documento:
Article