Drosophila CTP synthase can form distinct substrate- and product-bound filaments
Zhou, Xian1; Guo, Chen-Jun1; Hu, Huan-Huan1,2,3; Zhong, Jiale1,2,3; Sun, Qianqian1,4; Liu, Dandan1,4; Zhou, Shuang1,2,3; Chang, Chia Chun1; Liu, Ji-Long1
2019-11-20
Source PublicationJOURNAL OF GENETICS AND GENOMICS
ISSN1673-8527
Volume46Issue:11Pages:537-545
Status已发表
DOI10.1016/j.jgg.2019.11.006
AbstractIntracellular compartmentation is a key strategy for the functioning of a cell. In 2010, several studies revealed that the metabolic enzyme CTP synthase (CTPS) can form filamentous structures termed cytoophidia in prokaryotic and eukaryotic cells. However, recent structural studies showed that CTPS only forms inactive product-bound filaments in bacteria while forming active substrate-bound filaments in eukaryotic cells. In this study, using negative staining and cryo-electron microscopy, we demonstrate that Drosophila CTPS, whether in substrate-bound or product-bound form, can form filaments. Our results challenge the previous model and indicate that substrate-bound and product-bound filaments can coexist in the same species. We speculate that the ability to switch between active and inactive cytoophidia in the same cells provides an additional layer of metabolic regulation. Copyright (C) 2020, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, and Genetics Society of China. Published by Elsevier Limited and Science Press. All rights reserved.
KeywordCTP synthase Drosophila Cytoophidium Cryo-EM
Indexed BySCI
Language英语
Funding ProjectNational Natural Science Foundation of China[31771490]
WOS Research AreaBiochemistry & Molecular Biology ; Genetics & Heredity
WOS SubjectBiochemistry & Molecular Biology ; Genetics & Heredity
WOS IDWOS:000509466100005
PublisherSCIENCE PRESS
EISSN1873-5533
WOS KeywordSYNTHETASE ; CYTOOPHIDIA
Original Document TypeArticle
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Cited Times [WOS]:0   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://kms.shanghaitech.edu.cn/handle/2MSLDSTB/105297
Collection生命科学与技术学院_PI研究组_刘冀珑组
iHuman研究所_公共科研平台_生命科学电镜平台
生命科学与技术学院_硕士生
生命科学与技术学院_本科生
Corresponding AuthorLiu, Ji-Long
Affiliation1.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China
2.Chinese Acad Sci, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.ShanghaiTech Univ, iHuman Inst, Shanghai 201210, Peoples R China
First Author AffilicationSchool of Life Science and Technology
Corresponding Author AffilicationSchool of Life Science and Technology
First Signature AffilicationSchool of Life Science and Technology
Recommended Citation
GB/T 7714
Zhou, Xian,Guo, Chen-Jun,Hu, Huan-Huan,et al. Drosophila CTP synthase can form distinct substrate- and product-bound filaments[J]. JOURNAL OF GENETICS AND GENOMICS,2019,46(11):537-545.
APA Zhou, Xian.,Guo, Chen-Jun.,Hu, Huan-Huan.,Zhong, Jiale.,Sun, Qianqian.,...&Liu, Ji-Long.(2019).Drosophila CTP synthase can form distinct substrate- and product-bound filaments.JOURNAL OF GENETICS AND GENOMICS,46(11),537-545.
MLA Zhou, Xian,et al."Drosophila CTP synthase can form distinct substrate- and product-bound filaments".JOURNAL OF GENETICS AND GENOMICS 46.11(2019):537-545.
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