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Toward the goal of efficient editing of farm animals for genetic improvements, this study explores an upgraded form of nuclease PE (uPEn). Based on the resolved structure of the NiV polymerase L-P complex, this study identified two conserved zinc-binding sites within the PRNTase domain and characterized the L-P interaction interface. Notably, the XD domain of P1 was stably positioned above the NTD entry channel. Mutagenesis experiments targeting these critical regions, combined with mini-replicon assay, revealed that disruption of these sites significantly impaired polymerase activity. These findings deepen the mechanistic understanding of NiV polymerase functionality and provide structural insights into key regulatory sites essential for viral RNA synthesis.
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Xue L, Chang T, Gui J, Li Z, Zhao H, Zou B, Lu J, Li M, Wen X, Gao S, Zhan P, Rong L, Feng L, Gong P, He J, Chen X, Xiong X
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