ArticleNucleic acids research2016
Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies on an elaborate interface.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed.
- A comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation.Nucleic acids research · 2026Article
- Highly conserved ribosome biogenesis pathways between human and yeast revealed by the MDN1-NLE1 interaction and NLE1 containing pre-60S subunits.Nucleic acids research · 2025Article
- Article
- Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation.EMBO reports · 2023Article
- Identification and characterization of sugar-regulated promoters in Chaetomium thermophilum.BMC biotechnology · 2023Article
- Mechanism of 5S RNP recruitment and helicase-surveilled rRNA maturation during pre-60S biogenesis.EMBO reports · 2023Article
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- Concurrent remodelling of nucleolar 60S subunit precursors by the Rea1 ATPase and Spb4 RNA helicase.eLife · 2023Article
- Sequence-specific remodeling of a topologically complex RNP substrate by Spb4.Nature structural & molecular biology · 2022Article
- RNA folding and functions of RNA helicases in ribosome biogenesis.RNA biology · 2022Review
- The ribosome assembly factor Nop53 has a structural role in the formation of nuclear pre-60S intermediates, affecting late maturation events.Nucleic acids research · 2021Article
- From Snapshots to Flipbook-Resolving the Dynamics of Ribosome Biogenesis with Chemical Probes.International journal of molecular sciences · 2020Review
- Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis.Biomolecules · 2019Review
- Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin-ligand-type complexes.Nature communications · 2019Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- Suppressor mutations in Rpf2-Rrs1 or Rpl5 bypass the Cgr1 function for pre-ribosomal 5S RNP-rotation.Nature communications · 2018Article
- NOP7 interacts with β-catenin and activates β-catenin/TCF signaling in hepatocellular carcinoma cells.OncoTargets and therapy · 2018Article
- Article
- The assembly factor Erb1 functions in multiple remodeling events during 60S ribosomal subunit assembly in S. cerevisiae.Nucleic acids research · 2017Article
- Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2.Structure (London, England : 1993) · 2017Article
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5 authors.
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Abstract
The complicated process of eukaryotic ribosome biogenesis involves about 200 assembly factors that transiently associate with the nascent pre-ribosome in a spatiotemporally ordered way. During the early steps of 60S subunit formation, several proteins, collectively called A3 cluster factors, participate in the removal of the internal transcribed spacer 1 (ITS1) from 27SA3 pre-rRNA. Among these factors is the conserved hetero-trimeric Nop7-Erb1-Ytm1 complex (or human Pes1-Bop1-Wdr12), which is removed from the evolving pre-60S particle by the AAA ATPase Rea1 to allow progression in the pathway. Here, we clarify how Ytm1 and Erb1 interact, which has implications for the release mechanism of both factors from the pre-ribosome. Biochemical studies show that Ytm1 and Erb1 bind each other via their ß-propeller domains. The crystal structure of the Erb1-Ytm1 heterodimer determined at 2.67Å resolution reveals an extended interaction surface between the propellers in a rarely observed binding mode. Structure-based mutations in the interface that impair the Erb1-Ytm1 interaction do not support growth, with specific defects in 60S subunit synthesis. Under these mutant conditions, it becomes clear that an intact Erb1-Ytm1 complex is required for 60S maturation and that loss of this stable interaction prevents ribosome production.
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