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作 者:Hui-Yun Liu Qi Zhao Tian-Peng Zhang Yue Wu Yun-Xia Xiong Shi-Ke Wang Yuan-Long Ge Jin-Hui He Peng Lv 欧田苗[2] Jia-Heng Tan Ding Li Lian-Quan Gu Jian Ren 赵勇[3] 黄志纾
机构地区:[1]不详 [2]中山大学药学院 [3]中山大学生命科学学院
出 处:《科学新闻》2017年第4期175-175,共1页Science News
基 金:国家自然科学基金委重点项目;广东省以及广州市科研项目的资金支持
摘 要:G-四链体是一种具有显著结构多态性的核酸特殊二级结构。细胞内精确的G-四链体构象形式及其与生物学功能的相关性一直存在争议和不清楚的地方,对端粒G-PU链体尤其如此。G-quadruplexes are specialized secondary structures in nucleic acids that possess significant conformational polymorphisms. The precise G-quadruplex conformations in vivo and their relevance to biological functions remain controversial and unclear, especially for telomeric G-quadruplexes. Here, we report a novel single-chain variable fragment (scFv) antibody, D1, with high binding selectivity for parallel G-quadruplexes in vitro and in vivo. Genome-wide chromatin immunoprecipitation using D1 and deep-sequencing revealed the consensus sequence for parallel G-quadruplex formation, which is characterized by G-rich sequence with a short loop size (< 3 nt). By using D1, telomeric parallel G-quadruplex was identified and its formation was regulated by small molecular ligands targeting and telomere replication. Together, parallel G-quadruplex specific antibody D1 was found to be a valuable tool for determination of G-quadruplex and its conformation, which will prompt further studies on the structure of G-quadruplex and its biological implication in vivo.
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