2. Academic Validation
  3. Structural snapshots of human pre-60S ribosomal particles before and after nuclear export

Structural snapshots of human pre-60S ribosomal particles before and after nuclear export

  • Nat Commun. 2020 Jul 15;11(1):3542. doi: 10.1038/s41467-020-17237-x.
Xiaomeng Liang 1 2,  Mei-Qing Zuo 3 4 5,  Yunyang Zhang 2,  Ningning Li 2,  Chengying Ma 2,  Meng-Qiu Dong 4 5,  Ning Gao 6
Affiliations

Affiliations

  • 1 State Key Laboratory of Membrane Biology, School of Life Science, Tsinghua University, 100084, Beijing, China.
  • 2 State Key Laboratory of Membrane Biology, Peking-Tsinghua Joint Centre for Life Sciences, School of Life Sciences, Peking University, 100871, Beijing, China.
  • 3 College of Biological Sciences, China Agricultural University, 100193, Beijing, China.
  • 4 National Institute of Biological Sciences, 102206, Beijing, China.
  • 5 Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, 100084, Beijing, China.
  • 6 State Key Laboratory of Membrane Biology, Peking-Tsinghua Joint Centre for Life Sciences, School of Life Sciences, Peking University, 100871, Beijing, China. [email protected].
PMID: 32669547 DOI: 10.1038/s41467-020-17237-x
Abstract

Ribosome biogenesis is an elaborate and energetically expensive program that involve two hundred protein factors in eukaryotes. Nuclear export of pre-ribosomal particles is one central step which also serves as an internal structural checkpoint to ensure the proper completion of nuclear assembly events. Here we present four structures of human pre-60S particles isolated through a nuclear export factor NMD3, representing assembly stages immediately before and after nuclear export. These structures reveal locations of a dozen of human factors, including an uncharacterized factor TMA16 localized between the 5S RNA and the P0 stalk. Comparison of these structures shows a progressive maturation for the functional regions, such as peptidyl transferase centre and peptide exit tunnel, and illustrate a sequence of factor-assisted rRNA maturation events. These data facilitate our understanding of the global conservation of ribosome assembly in eukaryotes and species-specific features of human assembly factors.

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