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Coupling of 5S RNP rotation with maturation of functional centers during large ribosomal subunit assembly

Author

Listed:
  • Jelena Micic

    (Carnegie Mellon University)

  • Yu Li

    (School of Life Science, Tsinghua University
    Peking University-Tsinghua University-National Institute of Biological Sciences Joint Graduate Program)

  • Shan Wu

    (School of Life Science, Tsinghua University
    Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, School of Life Sciences, Hubei University)

  • Daniel Wilson

    (Carnegie Mellon University)

  • Beril Tutuncuoglu

    (University of California)

  • Ning Gao

    (Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University)

  • John L. Woolford

    (Carnegie Mellon University)

Abstract

The protein composition and structure of assembling 60S ribosomal subunits undergo numerous changes as pre-ribosomes transition from the nucleolus to the nucleoplasm. This includes stable anchoring of the Rpf2 subcomplex containing 5S rRNA, rpL5, rpL11, Rpf2 and Rrs1, which initially docks onto the flexible domain V of rRNA at earlier stages of assembly. In this work, we tested the function of the C-terminal domain (CTD) of Rpf2 during these anchoring steps, by truncating this extension and assaying effects on middle stages of subunit maturation. The rpf2Δ255-344 mutation affects proper folding of rRNA helices H68-70 during anchoring of the Rpf2 subcomplex. In addition, several assembly factors (AFs) are absent from pre-ribosomes or in altered conformations. Consequently, major remodeling events fail to occur: rotation of the 5S RNP, maturation of the peptidyl transferase center (PTC) and the nascent polypeptide exit tunnel (NPET), and export of assembling subunits to the cytoplasm.

Suggested Citation

  • Jelena Micic & Yu Li & Shan Wu & Daniel Wilson & Beril Tutuncuoglu & Ning Gao & John L. Woolford, 2020. "Coupling of 5S RNP rotation with maturation of functional centers during large ribosomal subunit assembly," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17534-5
    DOI: 10.1038/s41467-020-17534-5
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