Impact Factor:15.7
DOI number:10.1021/jacs.0c10792
Journal:J. Am. Chem. Soc.
Abstract:G-Quadruplex (G4) is a noncanonical nucleic acid secondary structure with multiple biofunctions. Identifying G4-related proteins (G4RPs) is important for understanding the roles of G4 in biology. Current methods to identify G4RPs include discovery from specific biological processes or in vitro pull-down assays with specific G4 sequences. Here, we report an in vivo strategy used to identify G4RPs with extensive sequence tolerance based on G4 ligand-mediated cross-linking. Applying this method, we identified 114 and 281 G4RPs in SV589 and MM231 cells, respectively. The results successfully overlapped with all the pull-down assay literature. Through the electrophoretic mobility shift assay (EMSA), we identified some new G4- binding proteins. Moreover, enhanced cross-linking and immunoprecipitation (eCLIP) confirmed that one newly identified G4-binding protein, SERBP1, interacts with G4 in the cellular environment. The method we developed provides a new strategy for identifying proteins that interact with nucleic secondary structures in cells and benefit the study of their biological roles.
Co-author:Yuqi Chen, Qi Wang, Ziang Lu, Yage Chen, Kun Chen, Shaoqing Han, Zhengtian Fang, Ping Wang, Bifeng Yuan
First Author:Jinglei Xu, Haomiao Su
Correspondence Author:Xiang Zhou
Discipline:Natural Science
Document Type:J
Volume:143
Page Number:1917-1923
Translation or Not:no
Date of Publication:2021-01-20
Included Journals:SCI
Links to published journals:https://pubs.acs.org/doi/10.1021/jacs.0c10792