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Post-transcriptional spliceosomes are retained in nuclear speckles until splicing completion

Author

Listed:
  • Cyrille Girard

    (Max Planck Institute for Biophysical Chemistry)

  • Cindy L. Will

    (Max Planck Institute for Biophysical Chemistry)

  • Jianhe Peng

    (Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry
    Present address: Cancer Research UK Centre, Leeds Institute of Molecular Medicine, University of Leeds, Beckett Street, Leeds LS9 7TF, UK)

  • Evgeny M. Makarov

    (Max Planck Institute for Biophysical Chemistry
    Present address: Division of Biosciences, School of Health Science and Social Care, HWB107, Brunel University, Kingston Lane, Uxbridge UB8 3PG, UK)

  • Berthold Kastner

    (Max Planck Institute for Biophysical Chemistry)

  • Ira Lemm

    (Max Planck Institute for Biophysical Chemistry
    Present address: FAIR Joint Core Team, GSI Helmholtzzentrum für Schwerionenforschung GmbH, Planckstraße 1, D-64291 Darmstadt, Germany.)

  • Henning Urlaub

    (Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry
    University Medical Center Göttingen Bioanalytics)

  • Klaus Hartmuth

    (Max Planck Institute for Biophysical Chemistry)

  • Reinhard Lührmann

    (Max Planck Institute for Biophysical Chemistry)

Abstract

There is little quantitative information regarding how much splicing occurs co-transcriptionally in higher eukaryotes, and it remains unclear where precisely splicing occurs in the nucleus. Here we determine the global extent of co- and post-transcriptional splicing in mammalian cells, and their respective subnuclear locations, using antibodies that specifically recognize phosphorylated SF3b155 (P-SF3b155) found only in catalytically activated/active spliceosomes. Quantification of chromatin- and nucleoplasm-associated P-SF3b155 after fractionation of HeLa cell nuclei, reveals that ~80% of pre-mRNA splicing occurs co-transcriptionally. Active spliceosomes localize in situ to regions of decompacted chromatin, at the periphery of or within nuclear speckles. Immunofluorescence microscopy with anti-P-SF3b155 antibodies, coupled with transcription inhibition and a block in splicing after SF3b155 phosphorylation, indicates that post-transcriptional splicing occurs in nuclear speckles and that release of post-transcriptionally spliced mRNA from speckles is coupled to the nuclear mRNA export pathway. Our data provide new insights into when and where splicing occurs in cells.

Suggested Citation

  • Cyrille Girard & Cindy L. Will & Jianhe Peng & Evgeny M. Makarov & Berthold Kastner & Ira Lemm & Henning Urlaub & Klaus Hartmuth & Reinhard Lührmann, 2012. "Post-transcriptional spliceosomes are retained in nuclear speckles until splicing completion," Nature Communications, Nature, vol. 3(1), pages 1-12, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1998
    DOI: 10.1038/ncomms1998
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    Cited by:

    1. Robert Atkinson & Maria Georgiou & Chunbo Yang & Katarzyna Szymanska & Albert Lahat & Elton J. R. Vasconcelos & Yanlong Ji & Marina Moya Molina & Joseph Collin & Rachel Queen & Birthe Dorgau & Avril W, 2024. "PRPF8-mediated dysregulation of hBrr2 helicase disrupts human spliceosome kinetics and 5´-splice-site selection causing tissue-specific defects," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Adel Al Jord & Gaëlle Letort & Soline Chanet & Feng-Ching Tsai & Christophe Antoniewski & Adrien Eichmuller & Christelle Da Silva & Jean-René Huynh & Nir S. Gov & Raphaël Voituriez & Marie-Émilie Terr, 2022. "Cytoplasmic forces functionally reorganize nuclear condensates in oocytes," Nature Communications, Nature, vol. 13(1), pages 1-19, December.

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