Nature, volume 556, issue 7699, pages 126-129
Modular assembly of the nucleolar pre-60S ribosomal subunit
Sanghai Zahra Assur
1
,
Miller Linamarie
1, 2
,
Molloy Kelly R.
3
,
Barandun Jonas
1
,
Hunziker Mirjam
1
,
Chaker Margot Malik
1, 2
,
Wang Jun-Jie
3
,
Chait Brian T.
3
,
Klinge Sebastian
1
1
Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University, New York, USA
|
2
Tri-Institutional Training Program in Chemical Biology, The Rockefeller University, New York, USA
|
3
Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, USA
|
Publication type: Journal Article
Publication date: 2018-03-05
PubMed ID:
29512650
Multidisciplinary
Abstract
Cryo-electron microscopy structures of multiple states along the assembly pathway of the nucleolar pre-60S ribosomal subunit suggest that folding of the pre-ribosomal RNA and sequential binding of transient assembly factors are regulated by steric hindrance among these factors. Cryo-electron microscopy approaches provide unprecedented views of how large molecular complexes assemble in cells. Sebastian Klinge and colleagues used these techniques to analyse the formation of the large pre-60S ribosomal subunit at a resolution of 3.4 Å. These analyses show that the concerted activity of several assembly factors is important for the stabilization and remodelling of intermediate structures of RNA and proteins while avoiding premature folding states. Progress through sequential steps of this assembly pathway is needed to achieve the correct conformation of the polypeptide exit tunnel of the ribosome. Early co-transcriptional events during eukaryotic ribosome assembly result in the formation of precursors of the small (40S) and large (60S) ribosomal subunits1. A multitude of transient assembly factors regulate and chaperone the systematic folding of pre-ribosomal RNA subdomains. However, owing to a lack of structural information, the role of these factors during early nucleolar 60S assembly is not fully understood. Here we report cryo-electron microscopy (cryo-EM) reconstructions of the nucleolar pre-60S ribosomal subunit in different conformational states at resolutions of up to 3.4 Å. These reconstructions reveal how steric hindrance and molecular mimicry are used to prevent both premature folding states and binding of later factors. This is accomplished by the concerted activity of 21 ribosome assembly factors that stabilize and remodel pre-ribosomal RNA and ribosomal proteins. Among these factors, three Brix-domain proteins and their binding partners form a ring-like structure at ribosomal RNA (rRNA) domain boundaries to support the architecture of the maturing particle. The existence of mutually exclusive conformations of these pre-60S particles suggests that the formation of the polypeptide exit tunnel is achieved through different folding pathways during subsequent stages of ribosome assembly. These structures rationalize previous genetic and biochemical data and highlight the mechanisms that drive eukaryotic ribosome assembly in a unidirectional manner.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Sanghai Z. A. et al. Modular assembly of the nucleolar pre-60S ribosomal subunit // Nature. 2018. Vol. 556. No. 7699. pp. 126-129.
GOST all authors (up to 50)
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Sanghai Z. A., Miller L., Molloy K. R., Barandun J., Hunziker M., Chaker Margot M., Wang J., Chait B. T., Klinge S. Modular assembly of the nucleolar pre-60S ribosomal subunit // Nature. 2018. Vol. 556. No. 7699. pp. 126-129.
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TY - JOUR
DO - 10.1038/nature26156
UR - https://doi.org/10.1038%2Fnature26156
TI - Modular assembly of the nucleolar pre-60S ribosomal subunit
T2 - Nature
AU - Sanghai, Zahra Assur
AU - Miller, Linamarie
AU - Molloy, Kelly R.
AU - Barandun, Jonas
AU - Hunziker, Mirjam
AU - Chaker Margot, Malik
AU - Wang, Jun-Jie
AU - Chait, Brian T.
AU - Klinge, Sebastian
PY - 2018
DA - 2018/03/05 00:00:00
PB - Springer Nature
SP - 126-129
IS - 7699
VL - 556
PMID - 29512650
SN - 0028-0836
SN - 1476-4687
ER -
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@article{2018_Sanghai
author = {Zahra Assur Sanghai and Linamarie Miller and Kelly R. Molloy and Jonas Barandun and Mirjam Hunziker and Malik Chaker Margot and Jun-Jie Wang and Brian T. Chait and Sebastian Klinge},
title = {Modular assembly of the nucleolar pre-60S ribosomal subunit},
journal = {Nature},
year = {2018},
volume = {556},
publisher = {Springer Nature},
month = {mar},
url = {https://doi.org/10.1038%2Fnature26156},
number = {7699},
pages = {126--129},
doi = {10.1038/nature26156}
}
Cite this
MLA
Copy
Sanghai, Zahra Assur, et al. “Modular assembly of the nucleolar pre-60S ribosomal subunit.” Nature, vol. 556, no. 7699, Mar. 2018, pp. 126-129. https://doi.org/10.1038%2Fnature26156.