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Splicing fidelity revisited

Since the discovery of Prp16, a spliceosomal ATPase that alters the fidelity of splicing, many other ATPases associated with the spliceosome have been postulated to work similarly. The finding that Prp22, a DEAH-box ATPase, functions as a fidelity factor for the second step of splicing supports this hypothesis.

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Figure 1: Schematic of structural transitions facilitated by DExH/D-box ATPase/helicases during pre-mRNA splicing.
Figure 2: Schematic of various outcomes of Prp22-mediated spliceosomal transition, depending on the relative rates of second-step catalysis and ATP hydrolysis by Prp22.

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Query, C., Konarska, M. Splicing fidelity revisited. Nat Struct Mol Biol 13, 472–474 (2006). https://doi.org/10.1038/nsmb0606-472

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