Drosophila CTP synthase can form distinct substrate- and product-bound filaments.
Journal
Journal of genetics and genomics = Yi chuan xue bao
Journal Volume
46
Journal Issue
11
Start Page
537-545
ISSN
1673-8527
Date Issued
2019-11-20
Author(s)
Zhou, Xian
Guo, Chen-Jun
Hu, Huan-Huan
Zhong, Jiale
Sun, Qianqian
Liu, Dandan
Zhou, Shuang
Liu, Ji-Long
Abstract
Intracellular 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.
Subjects
CTP synthase
Cryo-EM
Cytoophidium
Drosophila
Publisher
Elsevier
Type
journal article