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

Author

Listed:
  • Carsten Boesler

    (MPI for Biophysical Chemistry
    Present address: Targos Molecular Pathology GmbH, Germaniastrasse 7, D-34119 Kassel, Germany)

  • 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
    Bioanalytics Group, Institute for Clinical Chemistry, University Medical Center Göttingen)

  • 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)

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.

Suggested Citation

  • Carsten Boesler & Norbert Rigo & Maria M. Anokhina & Marcel J. Tauchert & Dmitry E. Agafonov & Berthold Kastner & Henning Urlaub & Ralf Ficner & Cindy L. Will & Reinhard Lührmann, 2016. "A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity," Nature Communications, Nature, vol. 7(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11997
    DOI: 10.1038/ncomms11997
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    Cited by:

    1. Bella M. Ben-Oz & Feras E. Machour & Marian Nicola & Amir Argoetti & Galia Polyak & Rawad Hanna & Oded Kleifeld & Yael Mandel-Gutfreund & Nabieh Ayoub, 2023. "A dual role of RBM42 in modulating splicing and translation of CDKN1A/p21 during DNA damage response," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Xiechao Zhan & Yichen Lu & Yigong Shi, 2024. "Molecular basis for the activation of human spliceosome," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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