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Journal Article

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

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Fourmann,  J. B.
Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Lührmann,  R.
Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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2403764.pdf
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Citation

Tauchert, M. J., Fourmann, J. B., Lührmann, R., & Ficner, R. (2017). Structural insights into the mechanism of the DEAH-box RNA helicase Prp43. eLife, 6: e21510. doi:10.7554/eLife.21510.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-8E7B-4
Abstract
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 Prp43ATP-analogRNA 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 ?-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases.