ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2011
Use of a coenzyme by the glmS ribozyme-riboswitch suggests primordial expansion of RNA chemistry by small molecules.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 22 citations in OpenAlex.
- Optimized periphery-core interface increases fitness of the Bacillus subtilis glmS ribozyme.Nucleic acids research · 2024Article
- RNAs That Behave Like Prions.mSphere · 2020Article
- Recent advances and future trends of riboswitches: attractive regulatory tools.World journal of microbiology & biotechnology · 2018Review
- Unwinding the twister ribozyme: from structure to mechanism.Wiley interdisciplinary reviews. RNA · 2017Review
- A divalent cation-dependent variant of theRNA (New York, N.Y.) · 2017Article
- In vitro evolution of coenzyme-independent variants from the glmS ribozyme structural scaffold.Methods (San Diego, Calif.) · 2016Article
- Ribozyme Catalysis with a Twist: Active State of the Twister Ribozyme in Solution Predicted from Molecular Simulation.Journal of the American Chemical Society · 2016Article
- Decoding mechanisms by which silent codon changes influence protein biogenesis and function.The international journal of biochemistry & cell biology · 2015Review
- Article
- An in vitro evolved glmS ribozyme has the wild-type fold but loses coenzyme dependence.Nature chemical biology · 2013Article
- Rethinking quasispecies theory: From fittest type to cooperative consortia.World journal of biological chemistry · 2013Review
- The chemical origins of life and its early evolution: an introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Article
- Structure and mechanism of the T-box riboswitches.Wiley interdisciplinary reviews. RNAReview
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Abstract
The glmS ribozyme-riboswitch is the first known example of a naturally occurring catalytic RNA that employs a small molecule as a coenzyme. Binding of glucosamine-6-phosphate (GlcN6P) activates self-cleavage of the bacterial ribozyme, which is part of the mRNA encoding the metabolic enzyme GlcN6P-synthetase. Cleavage leads to negative feedback regulation. GlcN6P binds in the active site of the ribozyme, where its amine could function as a general acid and electrostatic catalyst. The ribozyme is pre-folded but inactive in the absence of GlcN6P, demonstrating it has evolved strict dependence on the exogenous small molecule. The ribozyme showcases the ability of RNA to co-opt non-covalently bound small molecules to expand its chemical repertoire. Analogue studies demonstrate that some molecules other than GlcN6P, such as l-serine (but not d-serine), can function as weak activators. This suggests how coenzyme use by RNA world ribozymes may have led to evolution of proteins. Primordial cofactor-dependent ribozymes may have evolved to bind their cofactors covalently. If amino acids were used as cofactors, this could have driven the evolution of RNA aminoacylation. The ability to make covalently bound peptide coenzymes may have further increased the fitness of such primordial ribozymes, providing a selective pressure for the invention of translation.
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