Drosophila CTP synthase can form distinct substrate- and product-bound filaments

Xian Zhou^{a, #},
Chen-Jun Guo^{a, #},
Huan-Huan Hu^{a, b, c},
Jiale Zhong^{a, b, c},
Qianqian Sun^{a, d},
Dandan Liu^{a, d},
Shuang Zhou^{a, b, c},
Chia Chun Chang^a,
Ji-Long Liu^{a
, ,}

a.
School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China
b.
Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, 200031, China
c.
University of Chinese Academy of Sciences, Beijing, 100049, China
d.
iHuman Institute, ShanghaiTech University, Shanghai, 201210, China

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Corresponding author: E-mail address: liujl3@shanghaitech.edu.cn (Ji-Long Liu)

These authors contributed to this work equally.

摘要

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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.
- CTP synthase /
- Cytoophidium /
- Cryo-EM
These authors contributed to this work equally.
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