ArticleScientific reports2017
Pwp2 mediates UTP-B assembly via two structurally independent domains.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
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- Quantitative DIA-based proteomics unveils ribosomal biogenesis pathways associated with increased final size in three-year-old Chinese mitten crab (Eriocheir sinensis).BMC genomics · 2025Article
- The novel pre-rRNA detection workflow "Riboprobing" allows simple identification of undescribed RNA species.RNA (New York, N.Y.) · 2024Article
- Diagnostic yield and novel candidate genes for neurodevelopmental disorders by exome sequencing in an unselected cohort with microcephaly.BMC genomics · 2023Article
- TRAP1 regulates the response of colorectal cancer cells to hypoxia and inhibits ribosome biogenesis under conditions of oxygen deprivation.International journal of oncology · 2022Article
- Structural Probing with MNase Tethered to Ribosome Assembly Factors Resolves Flexible RNA Regions within the Nascent Pre-Ribosomal RNA.Non-coding RNA · 2022Article
- Non-radioactive In Vivo Labeling of RNA with 4-Thiouracil.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The mTOR regulated RNA-binding protein LARP1 requires PABPC1 for guided mRNA interaction.Nucleic acids research · 2021Article
- Pol5 is required for recycling of small subunit biogenesis factors and for formation of the peptide exit tunnel of the large ribosomal subunit.Nucleic acids research · 2020Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- Assembly and structure of the SSU processome-a nucleolar precursor of the small ribosomal subunit.Current opinion in structural biology · 2018Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SSU processome constitutes a large ribonucleoprotein complex involved in the early steps of ribosome biogenesis. UTP-B is one of the first multi-subunit protein complexes that associates with the pre-ribosomal RNA to form the SSU processome. To understand the molecular basis of the hierarchical assembly of the SSU-processome, we have undergone a structural and functional analysis of the UTP-B subunit Pwp2p. We show that Pwp2p is required for the proper assembly of UTP-B and for a productive association of UTP-B with pre-rRNA. These two functions are mediated by two distinct structural domains. The N-terminal domain of Pwp2p folds into a tandem WD-repeat (tWD) that associates with Utp21p, Utp18p, and Utp6p to form a core complex. The CTDs of Pwp2p and Utp21p mediate the assembly of the heterodimer Utp12p:Utp13p that is required for the stable incorporation of the UTP-B complex in the SSU processome. Finally, we provide evidence suggesting a role of UTP-B as a platform for the binding of assembly factors during the maturation of 20S rRNA precursors.
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