Control of gene expression by a natural metabolite-responsive ribozyme
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- 1 March 2004
- journal article
- Published by Springer Nature in Nature
- Vol. 428 (6980) , 281-286
- https://doi.org/10.1038/nature02362
Abstract
Most biological catalysts are made of protein; however, eight classes of natural ribozymes have been discovered that catalyse fundamental biochemical reactions. The central functions of ribozymes in modern organisms support the hypothesis that life passed through an 'RNA world' before the emergence of proteins and DNA. We have identified a new class of ribozymes that cleaves the messenger RNA of the glmS gene in Gram-positive bacteria. The ribozyme is activated by glucosamine-6-phosphate (GlcN6P), which is the metabolic product of the GlmS enzyme. Additional data indicate that the ribozyme serves as a metabolite-responsive genetic switch that represses the glmS gene in response to rising GlcN6P concentrations. These findings demonstrate that ribozyme switches may have functioned as metabolite sensors in primitive organisms, and further suggest that modern cells retain some of these ancient genetic control systems.Keywords
This publication has 38 references indexed in Scilit:
- Adenine riboswitches and gene activation by disruption of a transcription terminatorNature Structural & Molecular Biology, 2003
- An mRNA structure in bacteria that controls gene expression by binding lysineGenes & Development, 2003
- Genetic Control by Metabolite‐Binding RiboswitchesChemBioChem, 2003
- An mRNA structure that controls gene expression by binding S-adenosylmethionineNature Structural & Molecular Biology, 2003
- Ribozyme speed limitsRNA, 2003
- Riboswitches Control Fundamental Biochemical Pathways in Bacillus subtilis and Other BacteriaPublished by Elsevier ,2003
- The antiquity of RNA-based evolutionNature, 2002
- Glucosamine-6-phosphate synthase—the multi-facets enzymeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2002
- The Structural Basis of Ribosome Activity in Peptide Bond SynthesisScience, 2000
- Ribozyme Structures and MechanismsAnnual Review of Biochemistry, 2000