The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis

The assembly of eukaryotic ribosomes is a hierarchical process involving about 200 biogenesis factors and a series of remodeling steps. The 5S RNP consisting of the 5S rRNA, RpL5 and RpL11 is recruited at an early stage, but has to rearrange during maturation of the pre-60S ribosomal subunit. Rpf2 a...

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Bibliographic Details
Published in:Nucleic acids research 2015-08, Vol.43 (14), p.7083-7095
Main Authors: Kharde, Satyavati, Calviño, Fabiola R, Gumiero, Andrea, Wild, Klemens, Sinning, Irmgard
Format: Article
Language:English
Subjects:
Aspergillus nidulans
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Fungal Proteins - physiology
Models, Molecular
Protein Binding
Protein Structure, Tertiary
Ribonucleoproteins - metabolism
Ribosomal Proteins - metabolism
Ribosome Subunits, Large, Eukaryotic - chemistry
Ribosome Subunits, Large, Eukaryotic - metabolism
RNA, Ribosomal, 5S - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
RNA-Binding Proteins - physiology
Structural Biology
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Summary:The assembly of eukaryotic ribosomes is a hierarchical process involving about 200 biogenesis factors and a series of remodeling steps. The 5S RNP consisting of the 5S rRNA, RpL5 and RpL11 is recruited at an early stage, but has to rearrange during maturation of the pre-60S ribosomal subunit. Rpf2 and Rrs1 have been implicated in 5S RNP biogenesis, but their precise role was unclear. Here, we present the crystal structure of the Rpf2-Rrs1 complex from Aspergillus nidulans at 1.5 Å resolution and describe it as Brix domain of Rpf2 completed by Rrs1 to form two anticodon-binding domains with functionally important tails. Fitting the X-ray structure into the cryo-EM density of a previously described pre-60S particle correlates with biochemical data. The heterodimer forms specific contacts with the 5S rRNA, RpL5 and the biogenesis factor Rsa4. The flexible protein tails of Rpf2-Rrs1 localize to the central protuberance. Two helices in the Rrs1 C-terminal tail occupy a strategic position to block the rotation of 25S rRNA and the 5S RNP. Our data provide a structural model for 5S RNP recruitment to the pre-60S particle and explain why removal of Rpf2-Rrs1 is necessary for rearrangements to drive 60S maturation.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkv640