期刊
CELL REPORTS
卷 24, 期 2, 页码 453-462出版社
CELL PRESS
DOI: 10.1016/j.celrep.2018.06.021
关键词
-
类别
资金
- NIH [TR01 GM104962, R01 GM097369, R00 HD057233, DP2 OD007371A, GM104962]
- Searle Scholar Award
- Russian Science Foundation [16-14-10377]
- Memorial Sloan Kettering Cancer Center Core Grant [P30 CA008748]
- Russian Science Foundation [16-14-10377] Funding Source: Russian Science Foundation
Prokaryotic Argonaute (Ago) proteins were recently shown to target foreign genetic elements, thus making them a perfect model for studies of interference mechanisms. Here, we study interactions of Rhodobacter sphaeroides Ago (RsAgo) with guide RNA (gRNA) and fully complementary or imperfect target DNA (tDNA) using biochemical and structural approaches. We show that RsAgo can specifically recognize both the first nucleotide in gRNA and complementary nucleotide in tDNA, and both interactions contribute to nucleic acid binding. Non-canonical pairs and bulges on the target strand can be accommodated by RsAgo with minimal perturbation of the duplex but significantly reduce RsAgo affinity to tDNA. Surprisingly, mismatches between gRNA and tDNA induce dissociation of the guide-target duplex from RsAgo. Our results reveal plasticity in the ability of Ago proteins to accommodate helical imperfections, show how this might affect the efficiency of RNA silencing, and suggest a potential mechanism for guide release and Ago recycling.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据