ArticleMethods (San Diego, Calif.)2016
In vitro evolution of coenzyme-independent variants from the glmS ribozyme structural scaffold.
Article in Methods (San Diego, Calif.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Regulatory RNAs inSynthetic and systems biotechnology · 2024Review
- Computational design and experimental verification of pseudoknotted ribozymes.RNA (New York, N.Y.) · 2023Article
- The fluorescent aptamer Squash extensively repurposes the adenine riboswitch fold.Nature chemical biology · 2022Article
- Structurally reconfigurable designer RNA structures for nanomachines.Biophysics reports · 2021Article
- Structure-based insights into self-cleavage by a four-way junctional twister-sister ribozyme.Nature communications · 2017Article
- A divalent cation-dependent variant of theRNA (New York, N.Y.) · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Uniquely among known natural ribozymes that cleave RNA sequence-specifically, the glmS ribozyme-riboswitch employs a small molecule, glucosamine-6-phosphate (GlcN6P) as a catalytic cofactor. In vitro selection was employed to search for coenzyme-independent variants of this ribozyme. In addition to shedding light on the catalytic mechanism of the ribozyme, such variants could resemble the evolutionary ancestors of the modern, GlcN6P-regulated ribozyme-riboswitch. A mutant pool was constructed such that the secondary structure elements, which define the triply-pseudoknotted global fold of the ribozyme, was preserved. A stringent selection scheme that relies on thiol-mercury affinity chromatography for separating active and inactive sequences ultimately yielded a triple mutant with a cleavage rate exceeding 3min(-1) that only requires divalent cations for activity. Mutational analysis demonstrated that a point reversion of the variant toward the wild-type sequence was sufficient to partially restore GlcN6P-dependence, suggesting that coenzyme dependence can be readily be acquired by RNAs that adopt the glmS ribozyme fold. The methods employed to perform this selection experiment are described in detail in this review.
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