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Quantitative dynamics and binding studies of the 20S proteasome by NMR

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  • Remco Sprangers

    (The University of Toronto)

  • Lewis E. Kay

    (The University of Toronto)

Abstract

The machinery used by the cell to perform essential biological processes is made up of large molecular assemblies. One such complex, the proteasome, is the central molecular machine for removal of damaged and misfolded proteins from the cell. Here we show that for the 670-kilodalton 20S proteasome core particle it is possible to overcome the molecular weight limitations that have traditionally hampered quantitative nuclear magnetic resonance (NMR) spectroscopy studies of such large systems. This is achieved by using an isotope labelling scheme where isoleucine, leucine and valine methyls are protonated in an otherwise highly deuterated background in concert with experiments that preserve the lifetimes of the resulting NMR signals. The methodology has been applied to the 20S core particle to reveal functionally important motions and interactions by recording spectra on complexes with molecular weights of up to a megadalton. Our results establish that NMR spectroscopy can provide detailed insight into supra-molecular structures over an order of magnitude larger than those routinely studied using methodology that is generally applicable.

Suggested Citation

  • Remco Sprangers & Lewis E. Kay, 2007. "Quantitative dynamics and binding studies of the 20S proteasome by NMR," Nature, Nature, vol. 445(7128), pages 618-622, February.
    • Handle: RePEc:nat:nature:v:445:y:2007:i:7128:d:10.1038_nature05512
    DOI: 10.1038/nature05512
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    Cited by:

    1. Yuki Toyama & Ichio Shimada, 2024. "NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Gogulan Karunanithy & Vaibhav Kumar Shukla & D. Flemming Hansen, 2024. "Solution-state methyl NMR spectroscopy of large non-deuterated proteins enabled by deep neural networks," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Diego F. Gauto & Pavel Macek & Duccio Malinverni & Hugo Fraga & Matteo Paloni & Iva Sučec & Audrey Hessel & Juan Pablo Bustamante & Alessandro Barducci & Paul Schanda, 2022. "Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    4. Fanindra Kumar Deshmukh & Gili Ben-Nissan & Maya A. Olshina & Maria G. Füzesi-Levi & Caley Polkinghorn & Galina Arkind & Yegor Leushkin & Irit Fainer & Sarel J. Fleishman & Dan Tawfik & Michal Sharon, 2023. "Allosteric regulation of the 20S proteasome by the Catalytic Core Regulators (CCRs) family," Nature Communications, Nature, vol. 14(1), pages 1-24, December.

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