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Small Self-cleaving Ribozymes
Open accessAbstract
The hammerhead, hairpin, hepatitis delta virus (HDV), Varkud Satellite (VS), and glmS ribozymes catalyze sequence-specific intramolecular cleavage of RNA. They range between 50 and 150 nucleotides in length, and are known as the "small self-cleaving ribozymes." Except for the glmS ribozyme that functions as a riboswitch in Gram-positive bacteria, they were originally discovered as domains of satellite RNAs. However, recent studies show that several of them are broadly distributed in genomes of organisms from many phyla. Each of these ribozymes has a unique overall architecture and active site organization. Crystal structures have revealed how RNA active sites can bind preferentially to the transition state of a reaction, whereas mechanistic studies have shown that nucleobases can efficiently perform general acid-base and electrostatic catalysis. This versatility explains the abundance of ribozymes in contemporary organisms and also supports a role for catalytic RNAs early in evolution.
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“The fidelity of the primer extension products resulting from the sequential addition of activated monomers, when catalyzed by activated oligomers, is sufficient to sustain a genome long enough to encode active ribozymes.”
From Nonenzymatic copying of RNA templates containing all four letters is catalyzed by activated oligonucleotides (2016) · cites this paper as Ferré-D'Amaré and Scott, 2010
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“Assuming an error threshold of one mutation per genome (Eigen, 1971), this value of fidelity allows for effective genome sizes of 50 nucleotides, long enough to produce functional ribozymes (Ferré-D'Amaré and Scott, 2010).”
From Nonenzymatic copying of RNA templates containing all four letters is catalyzed by activated oligonucleotides (2016) · cites this paper as Ferré-D'Amaré and Scott, 2010
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Metadata
- Authors
- Ferre-D'Amare, A. R., & Scott, W. G.
- Affiliations
- University of California, Santa Cruz (US)
- Corresponding author
- Scott, W. G.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-09-15
- Volume
- 2
- Issue
- 10
- Pages
- a003574-a003574
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC2944367
- OpenAlex
- W2105638515
- Cited by
- 205
- References
- 74
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 8 · 2023: 11 · 2022: 12 · 2021: 10 · 2020: 12 · 2019: 24 · 2018: 7 · 2017: 14 · 2016: 16 · 2015: 25 · 2014: 17 · 2013: 7 · 2012: 15
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- W. M. Keck Foundation
- National Institutes of Health (Z99 HL999999)
- National Heart, Lung, and Blood Institute (ZIAHL006102)
- National Institute of General Medical Sciences (GM63576, R01GM063576, R01GM087721)
- National Institute of Allergy and Infectious Diseases (AI043393, R01AI043393, R21AI043393)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- self-cleaving ribozymes, hammerhead ribozyme, hairpin ribozyme, hepatitis delta virus ribozyme, glmS ribozyme, riboswitches, RNA catalysis, crystal structure, ribozyme evolution, satellite RNA
- MeSH terms
- Hepatitis Delta Virus, Models, Molecular, Ribonuclease, Pancreatic, RNA, Catalytic, Catalytic Domain
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