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


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.

SUBMITTER: Liang X 

PROVIDER: S-EPMC7363849 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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

Liang Xiaomeng X   Zuo Mei-Qing MQ   Zhang Yunyang Y   Li Ningning N   Ma Chengying C   Dong Meng-Qiu MQ   Gao Ning N  

Nature communications 20200715 1


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 structure  ...[more]

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