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Elife. 2017 Jan 16;6. pii: e21510. doi: 10.7554/eLife.21510.

Structural insights into the mechanism of the DEAH-box RNA helicase Prp43.

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Department of Molecular Structural Biology, Institute for Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Göttingen, Germany.
Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.


The DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs. The exact modus operandi of Prp43 and of all other spliceosomal DEAH-box RNA helicases is still elusive. Here, we report crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43•ATP-analog•RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a β-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases.


Chaetomium thermophilum; DHX15; S. cerevisiae; X-ray crystallography; biochemistry; biophysics; rRNA biogenesis; spliceosome; structural biology

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