The study, published in the prestigious journal Nature, sheds light on the final stage of splicing, a crucial process in gene expression. During this phase, a complex molecular machinery called the spliceosome removes introns from the precursor RNA and joins exons to form mature messenger RNA. Once its task is completed, this complex must be released and disassembled so its components can be reused.
The research, led by Clemens Plaschka from the Institute of Molecular Pathology (IMP) in Vienna, utilized cryo-electron microscopy to identify two intermediate states of the human spliceosome. The findings describe the coordinated action of three RNA helicases (DHX15, Aquarius, and DHX35), molecular motors that rearrange the machinery and facilitate intron release, thereby enabling the complex's disassembly.
CABIMER, through its proteomics unit, provided crucial analyses for the proteomic aspects of this research. These findings significantly expand the understanding of splicing termination and offer new insights into how cells manage the disassembly of spliceosomes that may become stalled during RNA processing.
