Studies reveal the mechanism by which Agos proteins direct DNA strands to cleave target DNA strands
January 07, 2019 Source: Institute of Biophysics
Window._bd_share_config={ "common":{ "bdSnsKey":{ },"bdText":"","bdMini":"2","bdMiniList":false,"bdPic":"","bdStyle":" 0","bdSize":"16"},"share":{ }};with(document)0[(getElementsByTagName('head')[0]||body).appendChild(createElement('script')) .src='http://bdimg.share.baidu.com/static/api/js/share.js?v=89860593.js?cdnversion='+~(-new Date()/36e5)];On December 27, 2018, the Proceedings of the National Academy of Sciences (PNAS) published a paper entitled Two symmetric arginine residues play distinct roles in Thermus thermophilus Argonaute DNA guide strand-mediated DNA target cleavage. The paper clarifies the importance of two symmetric arginine involved in cleavage activity in the bacterial Agos protein at the atomic level.
RNA interference plays an important role in the regulation of gene expression and is ubiquitous in organisms. Ago protein binding small RNAs are a core component of RNA-induced silencing complexes that utilize small RNA guide strands to target complementary paired RNA molecules, degrade the mRNA of interest or inhibit translation of the mRNA of interest. Unlike eukaryotic Ago proteins that utilize RNA-guided stranding to target RNA molecules, numerous studies have shown that prokaryotic Ago proteins utilize DNA-guided strands to target DNA molecules with DNA-mediated DNA interference. TtAgo cleaves target DNA or RNA by RNase H-type mechanism. The change of Ago conformation promotes the conversion of active center between inactive state and active state, but the specific catalytic mechanism of Ago is still unclear. In this study, Wang Yanli, a research group of the Institute of Biophysics of the Chinese Academy of Sciences and his collaborators, found that two positively charged amino acids in TtAgo play an important role. In TtAgo, R545 is the major amino acid residue that stabilizes the conformation when cleavage of the target strand, while the effect of R486 is weak, indicating that glutamic acid refers to the amino acid residues on both sides when the Ago protein of different species cleaves the target strand. The molecular mechanism has changed.
The research was completed by Wang Yanli's research team and the Xuhui Huang Laboratory of the Hong Kong University of Science and Technology and the Yingkai Zhang Laboratory of New York University. Among them, Wang Yanli, a researcher at the Institute of Biophysics, Xuhui Huang, a professor at the Hong Kong University of Science and Technology, and Yingkai Zhang, a professor at New York University, are co-authors of the paper. The research was funded by the Ministry of Science and Technology, the National Natural Science Foundation, and the Chinese Academy of Sciences' Strategic Pilot Science and Technology Special (Class B). The Shanghai Synchrotron Radiation Source (SSRF) and the Japanese Synchrotron Radiation Source SPring-8 provided important technical support for the study.
Studies reveal the mechanism by which Agos proteins direct DNA strands to cleave target DNA strands
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