Cargando…
The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life
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 magnitu...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5872033/ https://www.ncbi.nlm.nih.gov/pubmed/29315240 http://dx.doi.org/10.3390/biology7010007 |
_version_ | 1783309748087554048 |
---|---|
author | Tanizawa, Kana Uchida, Sayuri Kurihara, Eri Umehara, Takuya Tamura, Koji |
author_facet | Tanizawa, Kana Uchida, Sayuri Kurihara, Eri Umehara, Takuya Tamura, Koji |
author_sort | Tanizawa, Kana |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5872033 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-58720332018-03-29 The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life Tanizawa, Kana Uchida, Sayuri Kurihara, Eri Umehara, Takuya Tamura, Koji Biology (Basel) Article 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. MDPI 2018-01-09 /pmc/articles/PMC5872033/ /pubmed/29315240 http://dx.doi.org/10.3390/biology7010007 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Tanizawa, Kana Uchida, Sayuri Kurihara, Eri Umehara, Takuya Tamura, Koji The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life |
title | The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life |
title_full | The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life |
title_fullStr | The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life |
title_full_unstemmed | The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life |
title_short | The Kiss Switch Brings Inactive R3C Ligase Ribozyme Back to Life |
title_sort | kiss switch brings inactive r3c ligase ribozyme back to life |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5872033/ https://www.ncbi.nlm.nih.gov/pubmed/29315240 http://dx.doi.org/10.3390/biology7010007 |
work_keys_str_mv | AT tanizawakana thekissswitchbringsinactiver3cligaseribozymebacktolife AT uchidasayuri thekissswitchbringsinactiver3cligaseribozymebacktolife AT kuriharaeri thekissswitchbringsinactiver3cligaseribozymebacktolife AT umeharatakuya thekissswitchbringsinactiver3cligaseribozymebacktolife AT tamurakoji thekissswitchbringsinactiver3cligaseribozymebacktolife AT tanizawakana kissswitchbringsinactiver3cligaseribozymebacktolife AT uchidasayuri kissswitchbringsinactiver3cligaseribozymebacktolife AT kuriharaeri kissswitchbringsinactiver3cligaseribozymebacktolife AT umeharatakuya kissswitchbringsinactiver3cligaseribozymebacktolife AT tamurakoji kissswitchbringsinactiver3cligaseribozymebacktolife |