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- W2290209659 abstract "Argonaute proteins (Ago) are core components of the RNA Induced Silencing Complex (RISC) that load and utilize small guide nucleic acids to silence mRNAs or cleave foreign DNAs. Despite the essential role of Ago in gene regulation and defense against virus, the molecular mechanism of guide-strand loading into Ago remains unclear. We explore such a mechanism in the bacterium Thermus thermophilus Ago (TtAgo), via a computational approach combining molecular dynamics, bias-exchange metadynamics, and protein–DNA docking. We show that apo TtAgo adopts multiple closed states that are unable to accommodate guide-DNA. Conformations able to accommodate the guide are beyond the reach of thermal fluctuations from the closed states. These results suggest an induced-fit dominant mechanism for guide-strand loading in TtAgo, drastically different from the two-step mechanism for human Ago 2 (hAgo2) identified in our previous study. Such a difference between TtAgo and hAgo2 is found to mainly originate from the distinct rigidity of their L1-PAZ hinge. Further comparison among known Ago structures from various species indicates that the L1-PAZ hinge may be flexible in general for prokaryotic Ago’s but rigid for eukaryotic Ago’s." @default.
- W2290209659 created "2016-06-24" @default.
- W2290209659 creator A5009607229 @default.
- W2290209659 creator A5034909064 @default.
- W2290209659 creator A5058993999 @default.
- W2290209659 creator A5059431543 @default.
- W2290209659 creator A5066822010 @default.
- W2290209659 creator A5074194686 @default.
- W2290209659 creator A5083071253 @default.
- W2290209659 date "2016-03-04" @default.
- W2290209659 modified "2023-10-13" @default.
- W2290209659 title "A Flexible Domain-Domain Hinge Promotes an Induced-fit Dominant Mechanism for the Loading of Guide-DNA into Argonaute Protein in <i>Thermus thermophilus</i>" @default.
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