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RNA splicing

Running rings around RNA

Nature volume 397, pages 655–656 (1999)Cite this article

Twenty years ago it was discovered that many people suffering from autoimmune diseases produce autoantibodies against Sm proteins — a family of proteins that bind to nuclear RNA. Subsequent work showed that the Sm proteins are involved in removing introns (regions not encoding the protein product) from messenger RNA precursors. Now, a study by Kambach et al.1 in Cell reports the crystal structures of two Sm protein complexes, and offers new insights into the architecture of the RNA splicing machinery.

Almost all genes in higher eukaryotes contain one or more introns that must be removed from pre-mRNA transcripts to produce functional mRNA. This RNA splicing takes place in the nucleus, and is catalysed by a large RNA-protein complex known as the spliceosome. In both yeast and mammals, the spliceosome contains conserved RNA-protein subunits, the U1, U2, U4/U6 and U5 small nuclear ribonucleoprotein particles (snRNPs, pronounced “snurps”). These snRNP subunits, together with additional protein-splicing factors, bind to conserved RNA sequence motifs at either end of the intron to form an active spliceosome.

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Figure 1: Organization of the spliceosome.
Figure 2: Proposed structure of the human Sm core complex1.

References

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  1. the Department of Biochemistry, University of Dundee, MSI/WTB Complex, Dow Street, DD1 5EH, Dundee, UK

    Angus I. Lamond

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  1. Angus I. Lamond
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Lamond, A. Running rings around RNA. Nature 397, 655–656 (1999). https://doi.org/10.1038/17697

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