5YMA

Crystal structure of ribosome assembly factor Efg1

5YMA の概要

• エントリーDOI: 10.2210/pdb5yma/pdb
• 分子名称: Putative rRNA processing protein (1 entity in total)
• 機能のキーワード: 90s pre-ribosome, ribosomal protein
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36362.65

構造登録者

Shu, S.,Ye, K. (登録日: 2017-10-21, 公開日: 2018-01-17, 最終更新日: 2024-11-20)

主引用文献

Shu, S.,Ye, K.
Structural and functional analysis of ribosome assembly factor Efg1.
Nucleic Acids Res., 46:2096-2106, 2018

PubMed Abstract: Ribosome biogenesis in eukaryotes is a complicated process that involves association and dissociation of numerous assembly factors and snoRNAs. The yeast small ribosomal subunit is first assembled into 90S pre-ribosomes in an ordered and dynamic manner. Efg1 is a protein with no recognizable domain that is associated with early 90S particles. Here, we determine the crystal structure of Efg1 from Chaetomium thermophilum at 3.3 Å resolution, revealing a novel elongated all-helical structure. Efg1 is not located in recently determined cryo-EM densities of 90S likely due to its low abundance in mature 90S. Genetic analysis in Saccharomyces cerevisiae shows that the functional core of Efg1 contains two helical hairpins composed of highly conserved residues. Depletion of Efg1 blocks 18S rRNA processing at sites A1 and A2, but not at site A0, and production of small ribosomal subunits. Efg1 is initially recruited by the 5' domain of 18S rRNA. Its absence disturbs the assembly of the 5' domain and inhibits release of U14 snoRNA from 90S. Our study shows that Efg1 is required for early assembly and reorganization of the 5' domain of 18S rRNA.

PubMed: 29361028
DOI: 10.1093/nar/gky011

実験手法

X-RAY DIFFRACTION (3.295 Å)