ArticleThe Journal of biological chemistry2016
The Crystal Structure of the Ubiquitin-like Domain of Ribosome Assembly Factor Ytm1 and Characterization of Its Interaction with the AAA-ATPase Midasin.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- WD40 Protein NLE1 as a Novel Diagnostic Biomarker Promoting Hepatocellular Carcinoma Proliferation.Clinical Medicine Insights. Oncology · 2025Article
- WDR12/RAC1 axis promoted proliferation and anti-apoptosis in colorectal cancer cells.Molecular and cellular biochemistry · 2024Article
- Arabidopsis NOTCHLESS plays an important role in root and embryo development.Plant signaling & behavior · 2023Article
- Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.International journal of molecular sciences · 2023Article
- Mechanism of 5S RNP recruitment and helicase-surveilled rRNA maturation during pre-60S biogenesis.EMBO reports · 2023Article
- SMAD4 Loss Induces c-MYC-Mediated NLE1 Upregulation to Support Protein Biosynthesis, Colorectal Cancer Growth, and Metastasis.Cancer research · 2022Article
- The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.eLife · 2022Article
- Genome-wide in silico characterization and stress induced expression analysis of BcL-2 associated athanogene (BAG) family in Musa spp.Scientific reports · 2022Article
- Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?International journal of molecular sciences · 2021Review
- Quantitative Proteomic Profiling Identifies a Potential Novel Chaperone Marker in Resistant Breast Cancer.Frontiers in oncology · 2021Article
- Long-range intramolecular allostery and regulation in the dynein-like AAA protein Mdn1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Multidomain ribosomal protein trees and the planctobacterial origin of neomura (eukaryotes, archaebacteria).Protoplasma · 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
- Structure and interactions of the archaeal motility repression module ArnA-ArnB that modulates archaellum gene expression inThe Journal of biological chemistry · 2019Article
- The AAA-ATPase MIDASIN 1 Functions in Ribosome Biogenesis and Is Essential for Embryo and Root Development.Plant physiology · 2019Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7.Nature communications · 2019Article
- NOP7 interacts with β-catenin and activates β-catenin/TCF signaling in hepatocellular carcinoma cells.OncoTargets and therapy · 2018Article
- Identification of WDR12 as a novel oncogene involved in hepatocellular carcinoma propagation.Cancer management and research · 2018Article
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3 authors at 2 institutions in 1 country.
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Abstract
The synthesis of eukaryotic ribosomes is a complex, energetically demanding process requiring the aid of numerous non-ribosomal factors, such as the PeBoW complex. The mammalian PeBoW complex, composed of Pes1, Bop1, and WDR12, is essential for the processing of the 32S preribosomal RNA. Previous work in Saccharomyces cerevisiae has shown that release of the homologous proteins in this complex (Nop7, Erb1, and Ytm1, respectively) from preribosomal particles requires Rea1 (midasin or MDN1 in humans), a large dynein-like protein. Midasin contains a C-terminal metal ion-dependent adhesion site (MIDAS) domain that interacts with the N-terminal ubiquitin-like (UBL) domain of Ytm1/WDR12 as well as the UBL domain of Rsa4/Nle1 in a later step in the ribosome maturation pathway. Here we present the crystal structure of the UBL domain of the WDR12 homologue from S. cerevisiae at 1.7 Å resolution and demonstrate that human midasin binds to WDR12 as well as Nle1 through their respective UBL domains. Midasin contains a well conserved extension region upstream of the MIDAS domain required for binding WDR12 and Nle1, and the interaction is dependent upon metal ion coordination because removal of the metal or mutation of residues that coordinate the metal ion diminishes the interaction. Mammalian WDR12 displays prominent nucleolar localization that is dependent upon active ribosomal RNA transcription. Based upon these results, we propose that release of the PeBoW complex and subsequent release of Nle1 by midasin is a well conserved step in the ribosome maturation pathway in both yeast and mammalian cells.
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