AI Article Synopsis
- The R3C ligase ribozyme facilitates the formation of a 3'-5'-phosphodiester bond through a nucleophilic attack by its 3'-hydroxyl group on triphosphates' 5'-α-phosphorus.
- In this study, truncating the R3C ribozyme significantly reduced its ligation activity, but introducing complementary kissing-loops reactivated it to about 20% of the full-length ribozyme's activity.
- The reactivation process relies on complex interactions between two ribozymes, suggesting that such mechanisms could have played a role in the evolution of functional RNA molecules.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5872033 | PMC |
| http://dx.doi.org/10.3390/biology7010007 | DOI Listing |
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Article Synopsis
- The R3C ligase ribozyme facilitates the formation of a 3'-5'-phosphodiester bond through a nucleophilic attack by its 3'-hydroxyl group on triphosphates' 5'-α-phosphorus.
- In this study, truncating the R3C ribozyme significantly reduced its ligation activity, but introducing complementary kissing-loops reactivated it to about 20% of the full-length ribozyme's activity.
- The reactivation process relies on complex interactions between two ribozymes, suggesting that such mechanisms could have played a role in the evolution of functional RNA molecules.
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