ArticleNucleic acids research2016
Integrative structural analysis of the UTPB complex, an early assembly factor for eukaryotic small ribosomal subunits.
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 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- A UTP3-dependent nucleolar translocation pathway facilitates pre-rRNA 5'ETS processing.Nucleic acids research · 2024Article
- Hypermethylation and Downregulation of UTP6 Are Associated With Stemness Properties, Chemoradiotherapy Resistance, and Prognosis in Rectal Cancer: A Co-expression Network Analysis.Frontiers in cell and developmental biology · 2021Article
- 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
- The SSU processome interactome inRNA (New York, N.Y.) · 2018Article
- 3.2-Å-resolution structure of the 90S preribosome before A1 pre-rRNA cleavage.Nature structural & molecular biology · 2017Article
- Pwp2 mediates UTP-B assembly via two structurally independent domains.Scientific reports · 2017Article
- Article
- Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome assembly is an essential and conserved cellular process in eukaryotes that requires numerous assembly factors. The six-subunit UTPB complex is an essential component of the 90S precursor of the small ribosomal subunit. Here, we analyzed the molecular architecture of UTPB using an integrative structural biology approach. We mapped the major interactions that associate each of six UTPB proteins. Crystallographic studies showed that Utp1, Utp21, Utp12 and Utp13 are evolutionarily related and form a dimer of dimers (Utp1-Utp21, Utp12-Utp13) through their homologous helical C-terminal domains. Molecular docking with crosslinking restraints showed that the WD domains of Utp12 and Utp13 are associated, as are the WD domains of Utp1, Utp21 and Utp18. Electron microscopy images of the entire UTPB complex revealed that it predominantly adopts elongated conformations and possesses internal flexibility. We also determined crystal structures of the WD domain of Utp18 and the HAT and deviant HAT domains of Utp6. A structural model of UTPB was derived based on these data.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.