ArticleProtein science : a publication of the Protein Society2017
Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 55 citations in OpenAlex.
- Comparative transcriptomics reveals stage-specific regulatory pathways of ear thickening in Auricularia polytricha.PloS one · 2026Article
- The function of Mak16 in ribosome biogenesis depends on its [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The snoRNP chaperone snR190 and the Npa1 complex form a macromolecular assembly required for 60S ribosomal subunit maturation.Nucleic acids research · 2025Article
- The Efg1-Bud22 dimer associates with the U14 snoRNP contacting the 5' rRNA domain of an early 90S pre-ribosomal particle.Nucleic acids research · 2024Article
- Structure of nascent 5S RNPs at the crossroad between ribosome assembly and MDM2-p53 pathways.Nature structural & molecular biology · 2023Article
- Identification and characterization of sugar-regulated promoters in Chaetomium thermophilum.BMC biotechnology · 2023Article
- The nucleoplasmic phase of pre-40S formation prior to nuclear export.Nucleic acids research · 2022Article
- Production of nascent ribosome precursors within the nucleolar microenvironment of Saccharomyces cerevisiae.Genetics · 2022Article
- The dual nature of the nucleolus.Genes & development · 2022Review
- Emergence of the primordial pre-60S from the 90S pre-ribosome.Cell reports · 2022Article
- Transformation of Chaetomium thermophilum and Affinity Purification of Native Thermostable Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Bud23 promotes the final disassembly of the small subunit Processome in Saccharomyces cerevisiae.PLoS genetics · 2020Article
- At least two molecules of the RNA helicase Has1 are simultaneously present in pre-ribosomes during ribosome biogenesis.Nucleic acids research · 2019Article
- Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.Protein & cell · 2019Article
- Proteins and RNA sequences required for the transition of the t-Utp complex into the SSU processome.FEMS yeast research · 2019Article
- Utp14 interaction with the small subunit processome.RNA (New York, N.Y.) · 2018Article
- The Npa1p complex chaperones the assembly of the earliest eukaryotic large ribosomal subunit precursor.PLoS genetics · 2018Article
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Authors and funding
18 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome biogenesis in eukaryotic cells is a highly dynamic and complex process innately linked to cell proliferation. The assembly of ribosomes is driven by a myriad of biogenesis factors that shape pre-ribosomal particles by processing and folding the ribosomal RNA and incorporating ribosomal proteins. Biochemical approaches allowed the isolation and characterization of pre-ribosomal particles from Saccharomyces cerevisiae, which lead to a spatiotemporal map of biogenesis intermediates along the path from the nucleolus to the cytoplasm. Here, we cloned almost the entire set (∼180) of ribosome biogenesis factors from the thermophilic fungus Chaetomium thermophilum in order to perform an in-depth analysis of their protein-protein interaction network as well as exploring the suitability of these thermostable proteins for structural studies. First, we performed a systematic screen, testing about 80 factors for crystallization and structure determination. Next, we performed a yeast 2-hybrid analysis and tested about 32,000 binary combinations, which identified more than 1000 protein-protein contacts between the thermophilic ribosome assembly factors. To exemplary verify several of these interactions, we performed biochemical reconstitution with the focus on the interaction network between 90S pre-ribosome factors forming the ctUTP-A and ctUTP-B modules, and the Brix-domain containing assembly factors of the pre-60S subunit. Our work provides a rich resource for biochemical reconstitution and structural analyses of the conserved ribosome assembly machinery from a eukaryotic thermophile.
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