Abstract
Argonaute (AGO) proteins play central roles in nucleic acid-guided interference that regulates gene expression and defend against foreign genetic elements in all life. Although much progress has been made with respect to the function of argonaute proteins in target recognition and cleavage, the detailed mechanism of their biological functions is not fully understood. Here, using atomic force microscopy-based single-molecule force spectroscopy, we studied target-guide dissociation in the absence or presence of Thermus thermophilus AGO (TtAGO). Our results indicated that AGO changed the fundamental properties of target-guide interaction. Dissociation of the target from the guide is easier in the lateral direction of the nucleic acid in the presence of AGO protein but harder in the longitudinal direction. Our results support the idea that one-dimensional diffusion of the RNA-induced silencing complex (RISC) along the target strand is more efficient than three-dimensional diffusion and explain the priority of RISC binding over the ribosome complex during translation elongation.
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