ArticleBiochemistry2010
The human HDV-like CPEB3 ribozyme is intrinsically fast-reacting.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- Structure and mechanism of HDV ribozymes revealing Lewis acid catalysis by a metal ion.Nature communications · 2026Article
- CHiTA: A scarless high-throughput pipeline for characterization of ribozymes.Methods (San Diego, Calif.) · 2025Article
- Direct testing of natural twister ribozymes from over a thousand organisms reveals a broad tolerance for structural imperfections.Nucleic acids research · 2024Article
- Inhibition ofeLife · 2024Article
- Article
- The Metabolome Weakens RNA Thermodynamic Stability and Strengthens RNA Chemical Stability.Biochemistry · 2022Article
- Predicting higher-order mutational effects in an RNA enzyme by machine learning of high-throughput experimental data.Frontiers in molecular biosciences · 2022Article
- RNA multimerization as an organizing force for liquid-liquid phase separation.RNA (New York, N.Y.) · 2022Review
- Strategies for Covalent Labeling of Long RNAs.Chembiochem : a European journal of chemical biology · 2021Review
- Experimental Resurrection of Ancestral Mammalian CPEB3 Ribozymes Reveals Deep Functional Conservation.Molecular biology and evolution · 2021Article
- Accurate inference of the full base-pairing structure of RNA by deep mutational scanning and covariation-induced deviation of activity.Nucleic acids research · 2020Article
- Design of highly active double-pseudoknotted ribozymes: a combined computational and experimental study.Nucleic acids research · 2019Article
- Cellular conditions of weakly chelated magnesium ions strongly promote RNA stability and catalysis.Nature communications · 2018Article
- Topological constraints of structural elements in regulation of catalytic activity in HDV-like self-cleaving ribozymes.Scientific reports · 2016Article
- Secondary structure confirmation and localization of Mg2+ ions in the mammalian CPEB3 ribozyme.RNA (New York, N.Y.) · 2016Article
- Generation of functional RNAs from inactive oligonucleotide complexes by non-enzymatic primer extension.Journal of the American Chemical Society · 2015Article
- Four RNA families with functional transient structures.RNA biology · 2015Article
- Solution structure and metal ion binding sites of the human CPEB3 ribozyme's P4 domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Single molecule fluorescence approaches shed light on intracellular RNAs.Chemical reviews · 2014Review
- Molecular crowding favors reactivity of a human ribozyme under physiological ionic conditions.Biochemistry · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Self-cleaving RNAs have recently been identified in mammalian genomes. A small ribozyme related in structure to the hepatitis delta virus (HDV) ribozyme occurs in a number of mammals, including chimpanzees and humans, within an intron of the CPEB3 gene. The catalytic mechanisms for the CPEB3 and HDV ribozymes appear to be similar, generating cleavage products with 5'-hydroxyl and 2',3'-cyclic phosphate termini; nonetheless, the cleavage rate reported for the CPEB3 ribozyme is more than 6000-fold slower than for the fastest HDV ribozyme. Herein, we use full-length RNA and cotranscriptional self-cleavage assays to compare reaction rates among human CPEB3, chimp CPEB3, and HDV ribozymes. Our data reveal that a single base change of the upstream flanking sequence, which sequesters an intrinsically weak P1.1 pairing in a misfold, increases the rate of the wild-type human CPEB3 ribozyme by approximately 250-fold; thus, the human ribozyme is intrinsically fast-reacting. Secondary structure determination and native gel analyses reveal that the cleaved population of the CPEB3 ribozyme has a single, secondary structure that closely resembles the HDV ribozyme. In contrast, the precleavage population of the CPEB3 ribozyme appears to have a more diverse secondary structure, possibly reflecting misfolding with the upstream sequence and dynamics intrinsic to the ribozyme. Prior identification of expressed sequence tags (ESTs) in human cells indicated that cleavage activity of the human ribozyme is tissue-specific. It is therefore possible that cellular factors interact with regions upstream of the CPEB3 ribozyme to unmask its high intrinsic reactivity.
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