5BY8

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

5BY8 の概要

• エントリーDOI: 10.2210/pdb5by8/pdb
• 分子名称: Rpf2, Rrs1 (3 entities in total)
• 機能のキーワード: ribosome biogenesis, brix domain, protein-rna interaction, 5s rnp, protein complex, biosynthetic protein
• 由来する生物種: Emericella nidulans FGSC A4; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35452.75

構造登録者

Kharde, S.,Calvino, F.R.,Gumiero, A.,Wild, K.,Sinning, I. (登録日: 2015-06-10, 公開日: 2015-07-08, 最終更新日: 2024-11-06)

主引用文献

Kharde, S.,Calvino, F.R.,Gumiero, A.,Wild, K.,Sinning, I.
The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis.
Nucleic Acids Res., 43:7083-7095, 2015

PubMed Abstract: 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.

PubMed: 26117542
DOI: 10.1093/nar/gkv640

実験手法

X-RAY DIFFRACTION (1.515 Å)