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Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68

Author

Listed:
  • Mikael Feracci

    (University of Leicester)

  • Jaelle N. Foot

    (University of Leicester)

  • Sushma N. Grellscheid

    (Institute of Genetic Medicine, Newcastle University, Central Parkway
    Present address: School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, UK)

  • Marina Danilenko

    (Institute of Genetic Medicine, Newcastle University, Central Parkway)

  • Ralf Stehle

    (Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München)

  • Oksana Gonchar

    (University of Leicester)

  • Hyun-Seo Kang

    (Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
    Institute of Structural Biology, Helmholtz Zentrum München)

  • Caroline Dalgliesh

    (Institute of Genetic Medicine, Newcastle University, Central Parkway)

  • N. Helge Meyer

    (Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
    Institute of Structural Biology, Helmholtz Zentrum München
    Present address: Department of General and Visceral Surgery, European Medical School, Klinikum Oldenburg, DE-26133 Oldenburg, Germany)

  • Yilei Liu

    (Institute of Genetic Medicine, Newcastle University, Central Parkway
    Present address: Department of Microbiology, Institute of Plant Biology, University of Zürich, Zollikerstrasse 107, CH-8008 Zürich, Switzerland)

  • Albert Lahat

    (School of Biological and Biomedical Sciences, University of Durham)

  • Michael Sattler

    (Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
    Institute of Structural Biology, Helmholtz Zentrum München)

  • Ian C. Eperon

    (University of Leicester)

  • David J. Elliott

    (Institute of Genetic Medicine, Newcastle University, Central Parkway)

  • Cyril Dominguez

    (University of Leicester)

Abstract

Sam68 and T-STAR are members of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins. T-STAR is a tissue-specific paralogue that regulates the alternative splicing of neuronal pre-mRNAs. STAR proteins differ from most splicing factors, in that they contain a single RNA-binding domain. Their specificity of RNA recognition is thought to arise from their property to homodimerize, but how dimerization influences their function remains unknown. Here, we establish at atomic resolution how T-STAR and Sam68 bind to RNA, revealing an unexpected mode of dimerization different from other members of the STAR family. We further demonstrate that this unique dimerization interface is crucial for their biological activity in splicing regulation, and suggest that the increased RNA affinity through dimer formation is a crucial parameter enabling these proteins to select their functional targets within the transcriptome.

Suggested Citation

  • Mikael Feracci & Jaelle N. Foot & Sushma N. Grellscheid & Marina Danilenko & Ralf Stehle & Oksana Gonchar & Hyun-Seo Kang & Caroline Dalgliesh & N. Helge Meyer & Yilei Liu & Albert Lahat & Michael Sat, 2016. "Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68," Nature Communications, Nature, vol. 7(1), pages 1-12, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10355
    DOI: 10.1038/ncomms10355
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