In:
eLife, eLife Sciences Publications, Ltd, Vol. 6 ( 2017-01-16)
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 β-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.21510.001
DOI:
10.7554/eLife.21510.002
DOI:
10.7554/eLife.21510.003
DOI:
10.7554/eLife.21510.004
DOI:
10.7554/eLife.21510.005
DOI:
10.7554/eLife.21510.006
DOI:
10.7554/eLife.21510.007
DOI:
10.7554/eLife.21510.008
DOI:
10.7554/eLife.21510.009
DOI:
10.7554/eLife.21510.010
DOI:
10.7554/eLife.21510.011
DOI:
10.7554/eLife.21510.012
DOI:
10.7554/eLife.21510.013
DOI:
10.7554/eLife.21510.014
DOI:
10.7554/eLife.21510.015
DOI:
10.7554/eLife.21510.016
DOI:
10.7554/eLife.21510.017
DOI:
10.7554/eLife.21510.018
DOI:
10.7554/eLife.21510.019
DOI:
10.7554/eLife.21510.020
DOI:
10.7554/eLife.21510.021
DOI:
10.7554/eLife.21510.022
DOI:
10.7554/eLife.21510.023
DOI:
10.7554/eLife.21510.024
DOI:
10.7554/eLife.21510.037
DOI:
10.7554/eLife.21510.038
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2017
detail.hit.zdb_id:
2687154-3