The proline synthesis enzyme P5CS forms cytoophidia in Drosophila
脯氨酸合成酶 P5CS 在果蝇形成 cytoophidia作者机构:School of Life Science and TechnologyShanghaiTech UniversityShanghai201210China Institute of Biochemistry and Cell BiologyShanghai Institutes for Biologicai SciencesChinese Academy of SciencesShanghai200031China University of Chinese Academy of SciencesBeijing100049China MRC Functional Genomics UnitDepartment of PhysiologyAnatomy and GeneticsUniversity of OxfordOxford0X13PTUnited Kingdom iHuman InstituteShanghaiTech UniversityShanghai201210China
出 版 物:《Journal of Genetics and Genomics》 (遗传学报(英文版))
年 卷 期:2020年第47卷第3期
页 面:131-143页
核心收录:
学科分类:0710[理学-生物学] 07[理学] 071009[理学-细胞生物学] 09[农学] 0901[农学-作物学] 090102[农学-作物遗传育种]
基 金:supported by ShanghaiTech University,the UK Medical Research Council(Grant No.MC_UU_12021/3 and MC_U137788471) National Natural Science Foundation of China(Grant No.31771490)
主 题:CTPS Cytoophidium Drosophila Glutamate P5CS Proline
摘 要:Compartmentation of enzymes via filamentation has arisen as a mechanism for the regulation of *** 2010,three groups independently reported that CTP synthase(CTPS)can assemble into a filamentous structure termed the *** searching for CTPS-interacting proteins,here we perform a yeast two-hybrid screening of Drosophila proteins and identify a putative CTPS-interacting protein,△~1-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 *** of P5CS increases the length of CTPS ***,filamentation of CTPS affects the morphology of P5CS cytoophid ***,in vitro analyses confirm the filament-fo rming property of *** work links CTPS with P5CS,two enzymes involved in the rate-limiting steps in pyrimidine and proline biosynthesis,respectively.