Ontology highlight
ABSTRACT:
SUBMITTER: Fourmann JB
PROVIDER: S-EPMC4866824 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Fourmann Jean-Baptiste JB Dybkov Olexandr O Agafonov Dmitry E DE Tauchert Marcel J MJ Urlaub Henning H Ficner Ralf R Fabrizio Patrizia P Lührmann Reinhard R
eLife 20160426
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-dom ...[more]