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Nucleoside modification-based flexizymes with versatile activity for tRNA aminoacylation.
Zhang, Xin-Dan; Wang, Yi-Shen; Xiang, Hua; Bai, Li-Wen; Cheng, Peng; Li, Kai; Huang, Rong; Wang, Xiaolei; Lei, Xinxiang.
Affiliation
  • Zhang XD; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
  • Wang YS; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
  • Xiang H; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
  • Bai LW; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
  • Cheng P; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
  • Li K; College of Life Sciences, South-Central Minzu University, Wuhan, 430074, China.
  • Huang R; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
  • Wang X; State Key Laboratory of Applied Organic Chemistry, College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 730000, China.
  • Lei X; School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China. leixx@lzu.edu.cn.
Chem Commun (Camb) ; 60(12): 1607-1610, 2024 Feb 06.
Article in En | MEDLINE | ID: mdl-38230513
ABSTRACT
Extensive research has focused on genetic code reprogramming using flexizymes (Fxs), ribozymes enabling diverse tRNA acylation. Here we describe a nucleoside-modification strategy for the preparation of flexizyme variants derived from 2'-OMe, 2'-F, and 2'-MOE modifications with unique and versatile activities, enabling the charging of tRNAs with a broad range of substrates. This innovative strategy holds promise for synthetic biology applications, offering a robust pathway to expand the genetic code for diverse substrate incorporation.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: RNA, Catalytic / Transfer RNA Aminoacylation Language: En Journal: Chem Commun (Camb) Journal subject: QUIMICA Year: 2024 Document type: Article Affiliation country: China Country of publication: United kingdom
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: RNA, Catalytic / Transfer RNA Aminoacylation Language: En Journal: Chem Commun (Camb) Journal subject: QUIMICA Year: 2024 Document type: Article Affiliation country: China Country of publication: United kingdom