In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-04-26)
Abstract:
The DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s) are unknown. We show that Prp43 fused to Ntr1's G-patch motif (Prp43_Ntr1GP) is as efficient as the NTR in ILS disassembly, yielding identical dissociation products and recognizing its natural ILS target even in the absence of Ntr1’s C-terminal-domain (CTD) and Ntr2. Unlike the NTR, Prp43_Ntr1GP disassembles earlier spliceosomal complexes (A, B, Bact), indicating that Ntr2/Ntr1-CTD prevents NTR from disrupting properly assembled spliceosomes other than the ILS. The U2 snRNP-intron interaction is disrupted in all complexes by Prp43_Ntr1GP, and in the spliceosome contacts U2 proteins and the pre-mRNA, indicating that the U2 snRNP-intron interaction is Prp43’s major target.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.15564.001
DOI:
10.7554/eLife.15564.002
DOI:
10.7554/eLife.15564.003
DOI:
10.7554/eLife.15564.004
DOI:
10.7554/eLife.15564.005
DOI:
10.7554/eLife.15564.006
DOI:
10.7554/eLife.15564.007
DOI:
10.7554/eLife.15564.008
DOI:
10.7554/eLife.15564.009
DOI:
10.7554/eLife.15564.010
DOI:
10.7554/eLife.15564.011
DOI:
10.7554/eLife.15564.012
DOI:
10.7554/eLife.15564.013
DOI:
10.7554/eLife.15564.014
DOI:
10.7554/eLife.15564.015
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2016
detail.hit.zdb_id:
2687154-3