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原文連結
論文資訊
- 類型：已發表論文
- 日期：2022-01-12
摘要
Removal of the 5'-leader region is an essential step in the maturation of tRNA molecules in all domains of life. This reaction is catalyzed by various RNase P activities, ranging from ribonucleo蛋白質s with ribozyme activity to 蛋白質-only forms. In Escherichia coli, the efficiency of RNase P-mediated cleavage can be controlled by 計算ly designed riboswitch elements in a ligand-dependent way, where the 5'-leader sequence of a tRNA precursor is either sequestered in a hairpin structure or presented as a single-stranded region accessible for maturation. In the presented work, the regulatory potential of such artificial constructs is tested on different forms of eukaryotic RNase P enzymes-two 蛋白質-only RNase P enzymes (PRORP1 and PRORP2) from Arabidopsis thaliana and the ribonucleo蛋白質 of Homo sapiens.
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