Mechanisms of the Binding/Dissociation Acceleration of the Target-Guide Interaction by Thermus thermophilus Argonaute

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Prokaryotic Argonaute facilitates the target recognition process by the guide strand via a still unknown mechanism. Using single-molecule fluorescence resonance energy transfer and systematic mutagenesis of Thermus thermophilus Argonaute and guide-target base pairing, we study the kinetic roles of various structural features of guide strand in the prokaryotic Argonaute. We reveal that the 5'-end anchoring of the guide strand, and the sequence complementarity in the seed-and mid-regions greatly accelerate the target binding, and that this acceleration is due to the reduction of the entropic barrier of the binding process. Our data further suggest that the dynamic anchoring of the guide strand to the PAZ domain, which is coupled to target dissociation, does not accompany the partial unwinding of the guide-target duplex.
Publisher
WILEY-V C H VERLAG GMBH
Issue Date
2018-02
Language
English
Article Type
Article
Keywords

CRYSTAL-STRUCTURE; SILENCING COMPLEX; STRUCTURAL BASIS; SLICER ACTIVITY; PIWI PROTEIN; RNA; RECOGNITION; RISC; DNA; INTERFERENCE

Citation

BULLETIN OF THE KOREAN CHEMICAL SOCIETY, v.39, no.2, pp.167 - 173

ISSN
1229-5949
DOI
10.1002/bkcs.11362
URI
http://hdl.handle.net/10203/240379
Appears in Collection
BS-Journal Papers(저널논문)
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