SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome

The Journal of Biological Chemistry
J RappsilberM Mann

Abstract

Spliceosome assembly involves the sequential recruitment of small nuclear ribonucleoproteins (snRNPs) onto a pre-mRNA substrate. Although several non-snRNP proteins function during the binding of U1 and U2 snRNPs, little is known about the subsequent binding of the U4/U5/U6 tri-snRNP. A recent proteomic analysis of the human spliceosome identified SPF30 (Neubauer, G., King, A., Rappsilber, J., Calvio, C., Watson, M., Ajuh, P., Sleeman, J., Lamond, A., and Mann, M. (1998) Nat. Genet. 20, 46-50), a homolog of the survival of motor neurons (SMN) protein, as a spliceosome factor. We show here that SPF30 is a nuclear protein that associates with both U4/U5/U6 and U2 snRNP components. In the absence of SPF30, the preformed tri-snRNP fails to assemble into the spliceosome. Mass spectrometric analysis shows that a recombinant glutathione S-transferase-SPF30 fusion protein associates with complexes containing core Sm and U4/U5/U6 tri-snRNP proteins when added to HeLa nuclear extract, most strongly to U4/U6-90. The data indicate that SPF30 is an essential human splicing factor that may act to dock the U4/U5/U6 tri-snRNP to the A complex during spliceosome assembly or, alternatively, may act as a late assembly factor in both the tri-snRNP...Continue Reading

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Citations

Feb 20, 2002·Trends in Biochemical Sciences·Juri Rappsilber, Matthias Mann
Sep 15, 2011·Nature Reviews. Molecular Cell Biology·Chen ChenTony Pawson
Feb 2, 2010·Nature Structural & Molecular Biology·Marc SchneiderReinhard Lührmann
Nov 22, 2011·Nature Structural & Molecular Biology·Konstantinos TripsianesMichael Sattler
Jul 18, 2008·Human Molecular Genetics·Isabelle GouletJocelyn Côté
Jun 10, 2005·Nucleic Acids Research·Juana Maria Gonzalez-SantosJim Hu
Aug 15, 2002·Genome Research·Juri RappsilberMatthias Mann
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