ArticleNature communications2021
Structural basis for inhibition of the AAA-ATPase Drg1 by diazaborine.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Boron-Based Bioisosteres in Medicinal Chemistry: Advances in Heterocycles and Therapeutic.ChemMedChem · 2026Review
- ATAD2 as a Cancer Target: Insights into Its Structure, Functions, Mechanisms, and Drug Development.Cancers · 2025Review
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- The novel ribosome biogenesis inhibitor usnic acid blocks nucleolar pre-60S maturation.Nature communications · 2024Article
- K29-linked free polyubiquitin chains affect ribosome biogenesis and direct ribosomal proteins to the intranuclear quality control compartment.Molecular cell · 2024Article
- Ribosome biogenesis and function in development and disease.Development (Cambridge, England) · 2023Review
- Computational and mitochondrial functional studies of novel compound heterozygous variants in SPATA5 gene support a causal link with epileptogenic encephalopathy.Human genomics · 2023Article
- ATPase family AAA domain-containing protein 2 (ATAD2): From an epigenetic modulator to cancer therapeutic target.Theranostics · 2023Review
- Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition.Nature communications · 2022Article
- Communication network within the essential AAA-ATPase Rix7 drives ribosome assembly.PNAS nexus · 2022Article
- Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1.Nature structural & molecular biology · 2022Article
- Ribosome-Directed Therapies in Cancer.Biomedicines · 2022Review
- Labeling of heterochronic ribosomes reveals C1ORF109 and SPATA5 control a late step in human ribosome assembly.Cell reports · 2022Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The hexameric AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis and initiates cytoplasmic maturation of the large ribosomal subunit by releasing the shuttling maturation factor Rlp24. Drg1 monomers contain two AAA-domains (D1 and D2) that act in a concerted manner. Rlp24 release is inhibited by the drug diazaborine which blocks ATP hydrolysis in D2. The mode of inhibition was unknown. Here we show the first cryo-EM structure of Drg1 revealing the inhibitory mechanism. Diazaborine forms a covalent bond to the 2'-OH of the nucleotide in D2, explaining its specificity for this site. As a consequence, the D2 domain is locked in a rigid, inactive state, stalling the whole Drg1 hexamer. Resistance mechanisms identified include abolished drug binding and altered positioning of the nucleotide. Our results suggest nucleotide-modifying compounds as potential novel inhibitors for AAA-ATPases.
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