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Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel

Author

Listed:
  • Daniel M. Wilson

    (Carnegie Mellon University)

  • Yu Li

    (Tsinghua University
    Peking University-Tsinghua University-National Institute of Biological Sciences Joint Graduate Program)

  • Amber LaPeruta

    (Carnegie Mellon University)

  • Michael Gamalinda

    (Carnegie Mellon University
    Bayer AG, Strategy and Business Consulting)

  • Ning Gao

    (School of Life Sciences, Peking University)

  • John L. Woolford

    (Carnegie Mellon University)

Abstract

The nascent polypeptide exit tunnel (NPET) is a major functional center of 60S ribosomal subunits. However, little is known about how the NPET is constructed during ribosome assembly. We utilized molecular genetics, biochemistry, and cryo-electron microscopy (cryo-EM) to investigate the functions of two NPET-associated proteins, ribosomal protein uL4 and assembly factor Nog1, in NPET assembly. Structures of mutant pre-ribosomes lacking the tunnel domain of uL4 reveal a misassembled NPET, including an aberrantly flexible ribosomal RNA helix 74, resulting in at least three different blocks in 60S assembly. Structures of pre-ribosomes lacking the C-terminal extension of Nog1 demonstrate that this extension scaffolds the tunnel domain of uL4 in the NPET to help maintain stability in the core of pre-60S subunits. Our data reveal that uL4 and Nog1 work together in the maturation of ribosomal RNA helix 74, which is required to ensure proper construction of the NPET and 60S ribosomal subunits.

Suggested Citation

  • Daniel M. Wilson & Yu Li & Amber LaPeruta & Michael Gamalinda & Ning Gao & John L. Woolford, 2020. "Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel," Nature Communications, Nature, vol. 11(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18878-8
    DOI: 10.1038/s41467-020-18878-8
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