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2MVF

Structural insight into an essential assembly factor network on the pre-ribosome

Summary for 2MVF
Entry DOI10.2210/pdb2mvf/pdb
NMR InformationBMRB: 25265
DescriptorUncharacterized protein (1 entity in total)
Functional Keywordsribosome biogenesis, ribosomal protein
Biological sourceChaetomium thermophilum
Total number of polymer chains1
Total formula weight10317.97
Authors
Primary citationBaler, J.,Paternoga, H.,Holdermann, I.,Thoms, M.,Granneman, S.,Barrio-Garcia, C.,Nyarko, A.,Stier, G.,Clark, S.A.,Schraivogel, D.,Kallas, M.,Beckmann, R.,Tollervey, D.,Barbar, E.,Sinning, I.,Hurt, E.
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation.
J.Cell Biol., 207:481-498, 2014
Cited by
PubMed Abstract: Eukaryotic ribosome biogenesis involves ∼200 assembly factors, but how these contribute to ribosome maturation is poorly understood. Here, we identify a network of factors on the nascent 60S subunit that actively remodels preribosome structure. At its hub is Rsa4, a direct substrate of the force-generating ATPase Rea1. We show that Rsa4 is connected to the central protuberance by binding to Rpl5 and to ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2. Importantly, Nsa2 binds to helix 89 before relocation of helix 89 to the PTC. Structure-based mutations of these factors reveal the functional importance of their interactions for ribosome assembly. Thus, Rsa4 is held tightly in the preribosome and can serve as a "distribution box," transmitting remodeling energy from Rea1 into the developing ribosome. We suggest that a relay-like factor network coupled to a mechano-enzyme is strategically positioned to relocate rRNA elements during ribosome maturation.
PubMed: 25404745
DOI: 10.1083/jcb.201408111
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-18公开中

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