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Single Mutation in Hammerhead Ribozyme Favors Cleavage Activity with Manganese over Magnesium

1
Institut National de la Recherche Scientifique (INRS), Centre Armand Frappier Santé Biotechnologie, 531 boul. des Prairies, Laval, QB H7V 1B7, Canada
2
Department of Chemistry and Physics, Monmouth University, 400 Cedar Avenue, West Long Branch, NJ 07764, USA
*
Author to whom correspondence should be addressed.
Non-Coding RNA 2020, 6(1), 14; https://doi.org/10.3390/ncrna6010014 (registering DOI)
Received: 14 February 2020 / Revised: 16 March 2020 / Accepted: 18 March 2020 / Published: 20 March 2020
(This article belongs to the Collection Non-Coding RNA Methods)
Hammerhead ribozymes are one of the most studied classes of ribozymes so far, from both the structural and biochemical point of views. The activity of most hammerhead ribozymes is cation-dependent. Mg2+ is one of the most abundant divalent cations in the cell and therefore plays a major role in cleavage activity for most hammerhead ribozymes. Besides Mg2+, cleavage can also occur in the presence of other cations such as Mn2+. The catalytic core of hammerhead ribozymes is highly conserved, which could contribute to a preference of hammerhead ribozymes toward certain cations. Here, we show a naturally occurring variation in the catalytic core of hammerhead ribozymes, A6C, that can favor one metallic ion, Mn2+, over several other cations. View Full-Text
Keywords: manganese; magnesium; cation; RNA variants; C6 hammerhead variants; A6 manganese; magnesium; cation; RNA variants; C6 hammerhead variants; A6
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MDPI and ACS Style

Naghdi, M.R.; Boutet, E.; Mucha, C.; Ouellet, J.; Perreault, J. Single Mutation in Hammerhead Ribozyme Favors Cleavage Activity with Manganese over Magnesium. Non-Coding RNA 2020, 6, 14.

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