Structural insights into the mechanism of the DEAH-box RNA helicase Prp43
2017 | journal article. A publication with affiliation to the University of Göttingen.
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- Authors
- Tauchert, Marcel J.; Fourmann, Jean-Baptiste; Lührmann, Reinhard; Ficner, Ralf
- 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 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 b-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases.
- Issue Date
- 2017
- Journal
- eLife
- Organization
- Göttinger Zentrum für Molekulare Biowissenschaften
- ISSN
- 2050-084X
- Language
- English