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Int. J. Mol. Sci. 2015, 16(7), 14769-14785; doi:10.3390/ijms160714769

Conformational Dynamics of Ago-Mediated Silencing Processes

Institute of Molecular Medicine, Universitätsklinikum Schleswig-Holstein, Universität zu Lübeck, Lübeck 23538, Germany
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Author to whom correspondence should be addressed.
Academic Editor: Michael Ladomery
Received: 6 May 2015 / Revised: 10 June 2015 / Accepted: 17 June 2015 / Published: 1 July 2015
(This article belongs to the Special Issue RNA Interference)
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Abstract

Argonaute (Ago) proteins are key players of nucleic acid-based interference mechanisms. Their domains and structural organization are widely conserved in all three domains of life. However, different Ago proteins display various substrate preferences. While some Ago proteins are able to use several substrates, others are limited to a single one. Thereby, they were demonstrated to act specifically on their preferred substrates. Here, we discuss mechanisms of Ago-mediated silencing in relation to structural and biochemical insights. The combination of biochemical and structural information enables detailed analyses of the complex dynamic interplay between Ago proteins and their substrates. Especially, transient binding data allow precise investigations of structural transitions taking place upon Ago-mediated guide and target binding. View Full-Text
Keywords: Argonaute; mechanism; RNA interference; dynamics; kinetics; pre-steady state; steady state Argonaute; mechanism; RNA interference; dynamics; kinetics; pre-steady state; steady state
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Willkomm, S.; Restle, T. Conformational Dynamics of Ago-Mediated Silencing Processes. Int. J. Mol. Sci. 2015, 16, 14769-14785.

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