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The architecture of the Schizosaccharomyces pombe CCR4-NOT complex

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  • Marta Ukleja

    (Institute of Biochemistry and Biophysics, Polish Academy of Sciences
    Faculty of Biology, University of Warsaw
    Centro Nacional de Biotecnología (CNB-CSIC))

  • Jorge Cuellar

    (Centro Nacional de Biotecnología (CNB-CSIC))

  • Aleksandra Siwaszek

    (Institute of Biochemistry and Biophysics, Polish Academy of Sciences
    Faculty of Biology, University of Warsaw)

  • Joanna M. Kasprzak

    (Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw
    Bioinformatics Laboratory, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University)

  • Mariusz Czarnocki-Cieciura

    (Institute of Biochemistry and Biophysics, Polish Academy of Sciences
    Faculty of Biology, University of Warsaw)

  • Janusz M. Bujnicki

    (Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw
    Bioinformatics Laboratory, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University)

  • Andrzej Dziembowski

    (Institute of Biochemistry and Biophysics, Polish Academy of Sciences
    Faculty of Biology, University of Warsaw)

  • Jose M. Valpuesta

    (Centro Nacional de Biotecnología (CNB-CSIC))

Abstract

CCR4-NOT is a large protein complex present both in cytoplasm and the nucleus of eukaryotic cells. Although it is involved in a variety of distinct processes related to expression of genetic information such as poly(A) tail shortening, transcription regulation, nuclear export and protein degradation, there is only fragmentary information available on some of its nine subunits. Here we show a comprehensive structural characterization of the native CCR4-NOT complex from Schizosaccharomyces pombe. Our cryo-EM 3D reconstruction of the complex, combined with techniques such as immunomicroscopy, RNA-nanogold labelling, docking of the available high-resolution structures and models of different subunits and domains, allow us to propose its full molecular architecture. We locate all functionally defined domains endowed with deadenylating and ubiquitinating activities, the nucleus-specific RNA-interacting subunit Mmi1, as well as surfaces responsible for protein–protein interactions. This information provides insight into cooperation of the different CCR4-NOT complex functions.

Suggested Citation

  • Marta Ukleja & Jorge Cuellar & Aleksandra Siwaszek & Joanna M. Kasprzak & Mariusz Czarnocki-Cieciura & Janusz M. Bujnicki & Andrzej Dziembowski & Jose M. Valpuesta, 2016. "The architecture of the Schizosaccharomyces pombe CCR4-NOT complex," Nature Communications, Nature, vol. 7(1), pages 1-11, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10433
    DOI: 10.1038/ncomms10433
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    Cited by:

    1. Fabian Poetz & Joshua Corbo & Yevgen Levdansky & Alexander Spiegelhalter & Doris Lindner & Vera Magg & Svetlana Lebedeva & Jörg Schweiggert & Johanna Schott & Eugene Valkov & Georg Stoecklin, 2021. "RNF219 attenuates global mRNA decay through inhibition of CCR4-NOT complex-mediated deadenylation," Nature Communications, Nature, vol. 12(1), pages 1-19, December.

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