Isolation of an active step I spliceosome and composition of its RNP core

Sergey Bessonov, Maria Anokhina, Cindy L. Will, Henning Urlaub and Reinhard Lührmann ()
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Sergey Bessonov: and
Maria Anokhina: and
Cindy L. Will: and
Henning Urlaub: Bioanalytical Mass Spectrometry Group, Max Planck Institute of Biophysical Chemistry, D-37077 Göttingen, Germany
Reinhard Lührmann: and

Nature, 2008, vol. 452, issue 7189, 846-850

Abstract: Abstract Formation of catalytically active RNA structures within the spliceosome requires the assistance of proteins. However, little is known about the number and nature of proteins needed to establish and maintain the spliceosome’s active site. Here we affinity-purified human spliceosomal C complexes and show that they catalyse exon ligation in the absence of added factors. Comparisons of the composition of the precatalytic versus the catalytic spliceosome revealed a marked exchange of proteins during the transition from the B to the C complex, with apparent stabilization of Prp19–CDC5 complex proteins and destabilization of SF3a/b proteins. Disruption of purified C complexes led to the isolation of a salt-stable ribonucleoprotein (RNP) core that contained both splicing intermediates and U2, U5 and U6 small nuclear RNA plus predominantly U5 and human Prp19–CDC5 proteins and Prp19-related factors. Our data provide insights into the spliceosome’s catalytic RNP domain and indicate a central role for the aforementioned proteins in sustaining its catalytically active structure.

Date: 2008
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DOI: 10.1038/nature06842

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