ArticleBiochemistry2011
Rapid steps in the glmS ribozyme catalytic pathway: cation and ligand requirements.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 35 citations in OpenAlex.
- Characterization of the glmS Ribozymes from Listeria Monocytogenes and Clostridium Difficile.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- A cell-based ribozyme reporter system employing a chromosomally-integrated 5' exonuclease gene.BMC molecular and cell biology · 2021Article
- Metabolic engineering ofSynthetic and systems biotechnology · 2019Article
- Self-cleavage of theProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Corroboration of Zn(ii)-Mg(ii)-tertiary structure interplays essential for the optimal catalysis of a phosphorothiolate thiolesterase ribozyme.RSC advances · 2018Article
- Probing fast ribozyme reactions under biological conditions with rapid quench-flow kinetics.Methods (San Diego, Calif.) · 2017Article
- The GlcN6P cofactor plays multiple catalytic roles in the glmS ribozyme.Nature chemical biology · 2017Article
- Assessing the Potential Effects of Active Site MgThe journal of physical chemistry letters · 2016Article
- Two Divalent Metal Ions and Conformational Changes Play Roles in the Hammerhead Ribozyme Cleavage Reaction.Biochemistry · 2015Article
- Chemical feasibility of the general acid/base mechanism of glmS ribozyme self-cleavage.Biopolymers · 2015Article
- Role of the active site guanine in the glmS ribozyme self-cleavage mechanism: quantum mechanical/molecular mechanical free energy simulations.Journal of the American Chemical Society · 2015Article
- An in vitro evolved glmS ribozyme has the wild-type fold but loses coenzyme dependence.Nature chemical biology · 2013Article
- The glmS ribozyme cofactor is a general acid-base catalyst.Journal of the American Chemical Society · 2012Article
- An active-site guanine participates in glmS ribozyme catalysis in its protonated state.Journal of the American Chemical Society · 2011Article
- Two distinct catalytic strategies in the hepatitis δ virus ribozyme cleavage reaction.Biochemistry · 2011Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The glmS ribozyme is a conserved riboswitch found in numerous Gram-positive bacteria and responds to the cellular concentrations of glucosamine 6-phosphate (GlcN6P). GlcN6P binding promotes site-specific self-cleavage in the 5' UTR of the glmS mRNA, resulting in downregulation of gene expression. The glmS ribozyme has previously been shown to lack strong cation specificity when the rate-limiting folding step of the cleavage reaction pathway is measured. This does not provide data regarding cation and ligand specificities of the glmS ribozyme during the rapid ligand binding chemical catalysis events. Prefolding of the ribozyme in Mg(2+)-containing buffers effectively isolates the rapid ligand binding and catalytic events (k(obs) > 60 min(-1)) from rate-limiting folding (k(obs) < 4 min(-1)). Here we employ this experimental design to assay the cations and ligand requirements for rapid ligand binding and catalysis. We show that molar concentrations of monovalent cations are also capable of inducing the formation of the native GlcN6P binding structure but are unable to promote ligand binding and catalysis rates of >4 min(-1). Our data show that the sole obligatory role for divalent cations, for which there is crystallographic evidence, is coordination of the phosphate moiety of GlcN6P in the ligand-binding pocket. In further support of this hypothesis, our data show that a nonphosphorylated analogue of GlcN6P, glucosamine, is unable to promote rapid ligand binding and catalysis in the presence of divalent cations. Folding of the ribozyme is, therefore, relatively independent of cation identity, but the rapid initiation of catalysis upon the addition of ligand is stricter.
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