Poster presented by Team NUDT_CHINA 2020
Tianyi Zhang, Zhenyu Zhou, Changtai Xiao, Lunhao Ju, Xinlin Liu, Yongjiang Li, Huiying Liu, Qingyi Liu, Linjie Li, Ruoxi Wang, Yuxin Liu, Yingqian Ye, Junzi Gu, Haoyu Zhang, Yulan Chen, Zhiliang Pan, Hanxiao Feng, Guangyi Lin, Yanchen Gou, Yuxuan Wang, Weiqian Zhou.
Abstract
Exactitude temporal control of protein abundance is critical for the robustness and dynamics of synthetic circuits. While multiple approaches have been developed to manipulate the protein synthesis, few tools have been demonstrated to precisely control untagged protein degradation. Here, we present Predator Pro, a modularized and signal-controllable method for target protein degradation, on the basis of the Predator system we demonstrated in iGEM 2018-19. By rationally reengineer the Trim21 protein, we demonstrated that the interaction between Trim21 and antibody Fc domain can be replaced with other constitutive or inducible protein dimerization pairs. We demonstrated that constitutive DocS-Coh2 interaction or rapamycin-induced FRB-FKBP interaction enabled constitutive or drug-controlled degradation of untagged EGFP protein. As an effective expansion of the current synthetic biological tools for protein abundance control, this system may provide a modularized and convenient platform for controlled protein degradation, which might be applied in fundamental researches and clinical applications.