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• W2009723196 abstract "The L-21 Seal form of the Tetrahymena ribozyme acts as a sequence-specific endonuclease. This ribozyme has a homogeneous 5' end but a somewhat heterogeneous 3' end, as is typical of RNA synthesized by transcription in vitro. To produce a more homogeneous ribozyme for both structural and enzymological studies, a hammerhead ribozyme was inserted at the 3' end of the Tetrahymena ribozyme. During transcription the hammerhead moiety self-cleaves to produce the L-21 A Tetrahymena ribozyme, which ends at A410 with a 2',3'-cyclic phosphate terminus. The new ribozyme has endoribonuclease activity equivalent to that of L-21 Seal under conditions where binding of substrate is rate-limiting, as well as under conditions where chemical cleavage by guanosine is rate-limiting. However, the L-21 A has lost activity in oligo(C) dlsproportionation (e.g., 2 pC5-pC4 + pC6), consistent with the previous proposal that this reaction occurs predominantly through a covalent ribozyme-substrate intermediate involving the 3'-terminal hydroxyl group of the ribozyme. Formation of such an intermediate would be prevented by the 2',3'-cyclic phosphate terminus. Thus the L-21 A ribozyme has simplified enzymatic activity, being fully active as an endonuclease but blocked for disproportionation." @default.
• W2009723196 created "2016-06-24" @default.
• W2009723196 creator A5017573996 @default.
• W2009723196 creator A5035310999 @default.
• W2009723196 date "1991-01-01" @default.
• W2009723196 modified "2023-10-16" @default.
• W2009723196 title "A hammerhead ribozyme allows synthesis of a new form of the<i>Tetrahymena</i>ribozyme homogeneous in length with a 3' end blocked for transesterification" @default.
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• W2009723196 doi "https://doi.org/10.1093/nar/19.14.3875" @default.
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