Regulating enzymatic reactions in Escherichia coli utilizing light-responsive cellular compartments based on liquid-liquid phase separation

舱室(船) 化学 胞浆 合成生物学 细胞室 光遗传学 生物物理学 生物化学 生物 计算生物学 细胞 海洋学 神经科学 地质学
作者
Zikang Huang,Lize Sun,Genzhe Lu,Hongrui Liu,Zihan Zhai,S. H. Feng,Ji Gao,Chun‐Yu Chen,Chuheng Qing,Meng Fang,Bowen Chen,Jiale Fu,Xuan Wang,Guo‐Qiang Chen
标识
DOI:10.1101/2020.11.26.395616
摘要

Abstract Enzymatic reactions in cells are well organized into different compartments, among which protein-based membraneless compartments formed through liquid-liquid phase separation (LLPS) are believed to play important roles 1,2 . Hijacking them for our own purpose has promising applications in metabolic engineering 3 . Yet, it is still hard to precisely and dynamically control target enzymatic reactions in those compartments 4 . To address those problems, we developed Photo-Activated Switch in E. coli (PhASE), based on phase separating scaffold proteins and optogenetic tools. In this system, a protein of interest (POI) can be enriched up to 15-fold by LLPS-based compartments from cytosol within only a few seconds once activated by light, and become fully dispersed again within 15 minutes. Furthermore, we explored the potentiality of the LLPS-based compartment in enriching small organic molecules directly via chemical-scaffold interaction. With enzymes and substrates co-localized under light induction, the overall reaction efficiency could be enhanced. Using luciferin and catechol oxidation as model enzymatic reactions, we found that they could accelerate 2.3-fold and 1.6-fold, respectively, when regulated by PhASE. We anticipate our system to be an extension of the synthetic biology toolkit, facilitating rapid recruitment and release of POIs, and reversible regulation of enzymatic reactions.
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