Abstract
Humans share a comparable number of protein-coding genes with the simple roundworm Caenorhabditis elegans, yet we are arguably more sophisticated organisms. This difference in complexity is thanks to the spliceosome, an enormous piece of biochemical machinery found in the nucleus. The spliceosome cuts out unnecessary sequences of freshly transcribed RNA called introns and joins the remaining sections to form messenger RNA. The variable way that the spliceosome combines the nonintron RNA results in about 10 times as many proteins in human cells as the number of genes in our genome. Now, thanks to cryo-electron microscopy, researchers have a new, near-atomic-level view of this cellular machine in its precatalytic state, before it has decided to start splicing RNA (Nature 2017, DOI: 10.1038/nature22799). Dozens of proteins and five protein-RNA complexes, called ribonucleoproteins, come and go as the spliceosome prunes RNA after it has been transcribed from DNA and before protein production begins.
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