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- W342899305 abstract "Sequence-specific self-cleavage of RNAs by transesterification or hydrolysis of the target phosphodiester residue has been observed in a number of biological systems (Symons 1991; Pyle 1993). The hammerhead ribozyme is a relatively small RNA catalyst that is derived from a structural motif present in the RNA genomes of several plant pathogens, where it is believed that RNA-mediated cleavage events are an essential step in the viroid’s replication pathway (Forster and Symons 1987a; Symons 1989). The hammerhead complex consists of three helical stems (Forster and Symons 1987b; Uhlenbeck 1987) and includes eleven consensus nucleotides that appear to be responsible for the formation of a catalytically active domain (see Fig. 1; Ruffner et al. 1990). Nine of these conserved residues are nominally single-stranded, but may fold into an ordered structure upon binding of the substrate and/or the metal cofactor in order to stabilize the transition state resulting along the cleavage pathway. Cleavage of the RNA occurs by an internal transesterification reaction involving the 2′-hydroxyl adjacent to the scissile phosphodiester, generating a terminal 5′-hydroxyl fragment and a terminal 2′,3′-cyclic phosphate fragment (Uhlenbeck 1987).The reaction follows an in-line SN2 mechanism with inversion of configuration at the phosphorus center (van Tol et al. 1990; Slim and Gait 1991). Although in nature the hammerhead structures result from the folding of a single RNA strand, synthetic complexes composed of two or even three fragments also exhibit substantial cleavage activity and multiple turnover effects (Uhlenbeck 1987; Haseloff and Gerlach 1988; Koizumi et al. 1988; Jefferies and Symons 1989; Koizumi et al. 1989)." @default.
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- W342899305 date "1996-01-01" @default.
- W342899305 modified "2023-09-23" @default.
- W342899305 title "Probing the Cleavage Activity of the Hammerhead Ribozyme Using Analog Complexes" @default.
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- W342899305 doi "https://doi.org/10.1007/978-3-642-61202-2_11" @default.
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