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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-8E7B-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-8E7E-D
Genre: Journal Article

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Tauchert, M. J., Author
Fourmann, J. B.1, Author              
Lührmann, R.1, Author              
Ficner, R., Author
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1Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578576              

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 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.

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Language(s): eng - English
 Dates: 2017-01-16
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.21510
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Title: eLife
Source Genre: Journal
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Pages: 25 Volume / Issue: 6 Sequence Number: e21510 Start / End Page: - Identifier: -