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Structure of the human 80S ribosome

Author

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  • Heena Khatter

    (Centre for Integrative Biology (CBI), IGBMC (Institute of Genetics and of Molecular and Cellular Biology)
    Centre National de la Recherche Scientifique (CNRS)
    Institut National de la Santé et de la Recherche Médicale (INSERM) U964
    Université de Strasbourg)

  • Alexander G. Myasnikov

    (Centre for Integrative Biology (CBI), IGBMC (Institute of Genetics and of Molecular and Cellular Biology)
    Centre National de la Recherche Scientifique (CNRS)
    Institut National de la Santé et de la Recherche Médicale (INSERM) U964
    Université de Strasbourg)

  • S. Kundhavai Natchiar

    (Centre for Integrative Biology (CBI), IGBMC (Institute of Genetics and of Molecular and Cellular Biology)
    Centre National de la Recherche Scientifique (CNRS)
    Institut National de la Santé et de la Recherche Médicale (INSERM) U964
    Université de Strasbourg)

  • Bruno P. Klaholz

    (Centre for Integrative Biology (CBI), IGBMC (Institute of Genetics and of Molecular and Cellular Biology)
    Centre National de la Recherche Scientifique (CNRS)
    Institut National de la Santé et de la Recherche Médicale (INSERM) U964
    Université de Strasbourg)

Abstract

Ribosomes are translational machineries that catalyse protein synthesis. Ribosome structures from various species are known at the atomic level, but obtaining the structure of the human ribosome has remained a challenge; efforts to address this would be highly relevant with regard to human diseases. Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 Å, reaching 2.9 Å resolution in the most stable regions. It provides unprecedented insights into ribosomal RNA entities and amino acid side chains, notably of the transfer RNA binding sites and specific molecular interactions with the exit site tRNA. It reveals atomic details of the subunit interface, which is seen to remodel strongly upon rotational movements of the ribosomal subunits. Furthermore, the structure paves the way for analysing antibiotic side effects and diseases associated with deregulated protein synthesis.

Suggested Citation

  • Heena Khatter & Alexander G. Myasnikov & S. Kundhavai Natchiar & Bruno P. Klaholz, 2015. "Structure of the human 80S ribosome," Nature, Nature, vol. 520(7549), pages 640-645, April.
  • Handle: RePEc:nat:nature:v:520:y:2015:i:7549:d:10.1038_nature14427
    DOI: 10.1038/nature14427
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    Cited by:

    1. K. Shanmugha Rajan & Hava Madmoni & Anat Bashan & Masato Taoka & Saurav Aryal & Yuko Nobe & Tirza Doniger & Beathrice Galili Kostin & Amit Blumberg & Smadar Cohen-Chalamish & Schraga Schwartz & Andre , 2023. "A single pseudouridine on rRNA regulates ribosome structure and function in the mammalian parasite Trypanosoma brucei," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Chengwei Zeng & Yiren Jian & Soroush Vosoughi & Chen Zeng & Yunjie Zhao, 2023. "Evaluating native-like structures of RNA-protein complexes through the deep learning method," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    3. Casper Berger & Maud Dumoux & Thomas Glen & Neville B.-y. Yee & John M. Mitchels & Zuzana Patáková & Michele C. Darrow & James H. Naismith & Michael Grange, 2023. "Plasma FIB milling for the determination of structures in situ," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Gabriel Therizols & Zeina Bash-Imam & Baptiste Panthu & Christelle Machon & Anne Vincent & Julie Ripoll & Sophie Nait-Slimane & Mounira Chalabi-Dchar & Angéline Gaucherot & Maxime Garcia & Florian Laf, 2022. "Alteration of ribosome function upon 5-fluorouracil treatment favors cancer cell drug-tolerance," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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