Abstract
Using electrophoresis, sequencing and enzymatic digestion, we show that the group I intron from the cyanobacterium Anabaena sp. PCC 7120 catalyzes phosphodiester bond formation using a triphosphate on the 5'-terminal nucleotide, much like protein polymerases and engineered ribozymes. In the process, this ribozyme forms a unique circular RNA that incorporates the exogenous guanosine cofactor added during self-splicing. This finding may have relevance to a prebiotic RNA world and to modern biology.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anabaena / enzymology*
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Anabaena / genetics
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Catalysis
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Introns
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RNA Ligase (ATP) / metabolism*
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RNA, Catalytic / metabolism*
Substances
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RNA, Catalytic
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RNA Ligase (ATP)
Associated data
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PubChem-Substance/56413296
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PubChem-Substance/56413297
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PubChem-Substance/56413298
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PubChem-Substance/56413299
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PubChem-Substance/56413300
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PubChem-Substance/56413301
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PubChem-Substance/56413302
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PubChem-Substance/56413303
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PubChem-Substance/56413304
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PubChem-Substance/56413305