The proline synthesis enzyme P5CS forms cytoophidia in Drosophila  

作　　者：Bo Zhang Omür Y.Tastan Xian Zhou Chen-Jun Guo Xuyang Liu Aaron Thind Huan-Huan Hu Suwen Zhao Ji-Long Liu 

机构地区：[1]School of Life Science and Technology,ShanghaiTech University,Shanghai,201210,China [2]Institute of Biochemistry and Cell Biology,Shanghai Institutes for Biologicai Sciences,Chinese Academy of Sciences,Shanghai,200031,China [3]University of Chinese Academy of Sciences,Beijing,100049,China [4]MRC Functional Genomics Unit,Department of Physiology,Anatomy and Genetics,University of Oxford,Oxford,0X13PT,United Kingdom [5]iHuman Institute,ShanghaiTech University,Shanghai,201210,China

出　　处：《Journal of Genetics and Genomics》2020年第3期131-143,共13页遗传学报（英文版）

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)。

摘　　要：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,△~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 cytoophidia.Overexpression of P5CS increases the length of CTPS cytoophidia.Conversely,filamentation of CTPS affects the morphology of P5CS cytoophid ia.Finally,in vitro analyses confirm the filament-fo rming property of P5CS.Our work links CTPS with P5CS,two enzymes involved in the rate-limiting steps in pyrimidine and proline biosynthesis,respectively.

关 键 词：CTPS Cytoophidium DROSOPHILA GLUTAMATE P5CS PROLINE 

分 类 号：Q25[生物学—细胞生物学]