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The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life

1
Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijuku, Katsushika-ku, Tokyo 125-8585, Japan
2
Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan
*
Author to whom correspondence should be addressed.
Received: 8 November 2017 / Revised: 4 January 2018 / Accepted: 5 January 2018 / Published: 9 January 2018
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Abstract

R3C ligase ribozyme catalyzes the nucleophilic attack by a 3′-hydroxyl on a 5′-α-phosphorus of triphosphates to form a 3′-5′-phosphodiester bond. In the present study, although the truncation of R3C ribozyme was accompanied by a large reduction in ligation activity (decrease by two orders of magnitude compared to that of the ligated product of full-length R3C ribozyme after 18.5 h at 23 °C), the introduction of complementary seven-membered kissing-loops served as a “switch” to reactivate the truncated R3C ribozyme with approximately one-fifth of the activity of the full-length R3C ribozyme. This reactivation occurred in a trans-manner, and the grip region and substrate-binding site of the truncated R3C ribozyme were necessary to locate the substrate in the proper position for ligation with the other molecule. Reactivation resulted from complex tertiary interactions between two ribozymes, including kissing-loop interaction-induced annealing and the formation of a stable duplex. The drastic increase of the activity of poorly active ribozymes through the kissing-loop interaction may provide an important clue into the acquisition of substantial activity during the evolution of the RNA world. View Full-Text
Keywords: R3C ligase ribozyme; kissing-loop interaction; activity; RNA switch; RNA world R3C ligase ribozyme; kissing-loop interaction; activity; RNA switch; RNA world
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Tanizawa, K.; Uchida, S.; Kurihara, E.; Umehara, T.; Tamura, K. The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life. Biology 2018, 7, 7.

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