A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity

Carsten Boesler, Norbert Rigo, Maria M. Anokhina, Marcel J. Tauchert, Dmitry E. Agafonov, Berthold Kastner, Henning Urlaub, Ralf Ficner, Cindy L. Will () and Reinhard Lührmann ()
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Carsten Boesler: MPI for Biophysical Chemistry
Norbert Rigo: MPI for Biophysical Chemistry
Maria M. Anokhina: MPI for Biophysical Chemistry
Marcel J. Tauchert: Institute for Microbiology and Genetics, GZMB, Georg-August-Universität Göttingen
Dmitry E. Agafonov: MPI for Biophysical Chemistry
Berthold Kastner: MPI for Biophysical Chemistry
Henning Urlaub: Bioanalytical Mass Spectrometry Group, MPI for Biophysical Chemistry
Ralf Ficner: Institute for Microbiology and Genetics, GZMB, Georg-August-Universität Göttingen
Cindy L. Will: MPI for Biophysical Chemistry
Reinhard Lührmann: MPI for Biophysical Chemistry

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract The precise role of the spliceosomal DEAD-box protein Prp28 in higher eukaryotes remains unclear. We show that stable tri-snRNP association during pre-catalytic spliceosomal B complex formation is blocked by a dominant-negative hPrp28 mutant lacking ATPase activity. Complexes formed in the presence of ATPase-deficient hPrp28 represent a novel assembly intermediate, the pre-B complex, that contains U1, U2 and loosely associated tri-snRNP and is stalled before disruption of the U1/5′ss base pairing interaction, consistent with a role for hPrp28 in the latter. Pre-B and B complexes differ structurally, indicating that stable tri-snRNP integration is accompanied by substantial rearrangements in the spliceosome. Disruption of the U1/5′ss interaction alone is not sufficient to bypass the block by ATPase-deficient hPrp28, suggesting hPrp28 has an additional function at this stage of splicing. Our data provide new insights into the function of Prp28 in higher eukaryotes, and the requirements for stable tri-snRNP binding during B complex formation.

Date: 2016
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DOI: 10.1038/ncomms11997

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