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- W2156833843 abstract "We report here an in vitro selected ribozyme, KL17, which is active in charging amino acids on its own 5'-OH group. The ribozyme consists of two catalytic domains, one of which (consisting of P5/P6/L6) recognizes amino acid substrates based on the steric environment of the side chain, whereas the other recognizes an aminoacylated oligonucleotide. The secondary structure of this ambidextrous ribozyme arranges into a pseudoknot, where L6 docks onto the 3'-terminal single-stranded region. The formation of this pseudoknot structure brings the P6 region, in which the essential catalytic core is most likely embedded, into the proximity of the 5'-OH group. Our studies show that the P6-L6 domain can be separated from the main body of KL17 and the derived P6-L6 minihelix-loop RNA can act as a trans-aminoacylation catalyst. In this report, we also compare this ribozyme with an analogous aminoacylation system previously characterized in our laboratory and illuminate the similarities and differences between these catalytic systems." @default.
- W2156833843 created "2016-06-24" @default.
- W2156833843 creator A5016168396 @default.
- W2156833843 date "2002-05-15" @default.
- W2156833843 modified "2023-09-25" @default.
- W2156833843 title "Minihelix-loop RNAs: minimal structures for aminoacylation catalysts" @default.
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- W2156833843 doi "https://doi.org/10.1093/nar/30.10.2162" @default.
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