Abstract
Spliceosome Splicing of precursor messenger RNA (pre-mRNA) is carried out by the spliceosome, a highly dynamic, supramolecular complex that undergoes assembly, activation, catalysis, and disassembly. These essential spliceosome remodeling events are driven by a conserved family of adenosine triphosphatase (ATPase)/helicases. In the presence of its coactivator Spp2, the ATPase/helicase Prp2 associates with the activated spliceosome and translocates the single-stranded pre-mRNA toward its 3′ end. Bai et al. now report the cryo–electron microscopy structures of Prp2 both before and after recruitment into the activated spliceosome. These structures and the associated biochemical analysis reveal how Prp2 remodels the activated spliceosome and how Spp2 safeguards the function of Prp2. Science , this issue p. [eabe8863][1] [1]: /lookup/doi/10.1126/science.abe8863
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
