ArticleNature structural & molecular biology2019
Cryo-EM reveals active site coordination within a multienzyme pre-rRNA processing complex.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- End processing in NHEJ by Polymerase λ and PNKP is coordinated during short-range synapsis.Nature communications · 2026Article
- Structural insights into RNA phosphorylation by the RNase PNK module of the human rixosome complex.Nucleic acids research · 2026Article
- Human pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs.The Journal of biological chemistry · 2026Article
- Dual regulation of HEPN RNase in fused MNT-HEPN toxin-antitoxin systems via protein OligoAMPylation and oligomerization.Nucleic acids research · 2026Article
- Human Pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs.bioRxiv : the preprint server for biology · 2025Article
- PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex.Science advances · 2025Article
- Molecular insights into the overall architecture of human rixosome.Nature communications · 2025Article
- Coordinated DNA polymerization by Polγ and the region of LonP1 regulated proteolysis.Nucleic acids research · 2024Article
- The novel pre-rRNA detection workflow "Riboprobing" allows simple identification of undescribed RNA species.RNA (New York, N.Y.) · 2024Article
- Prokaryotic Argonaute nuclease cooperates with co-encoded RNase to acquire guide RNAs and target invader DNA.Nucleic acids research · 2024Article
- Structural and mechanistic insights into ribosomal ITS2 RNA processing by nuclease-kinase machinery.eLife · 2024Article
- Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation.EMBO reports · 2023Article
- Structural basis for pre-tRNA recognition and processing by the human tRNA splicing endonuclease complex.Nature structural & molecular biology · 2023Article
- Roles of ribosomal RNA in health and disease.Frontiers in RNA research · 2023Article
- Cryo-EM reveals the architecture of the PELP1-WDR18 molecular scaffold.Nature communications · 2022Article
- Communication network within the essential AAA-ATPase Rix7 drives ribosome assembly.PNAS nexus · 2022Article
- Structural insight and characterization of human Twinkle helicase in mitochondrial disease.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A comprehensive landscape of 60S ribosome biogenesis factors.Cell reports · 2022Article
- Transformation of Chaetomium thermophilum and Affinity Purification of Native Thermostable Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The ribosome assembly factor Nop53 has a structural role in the formation of nuclear pre-60S intermediates, affecting late maturation events.Nucleic acids research · 2021Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Ribosome assembly is a complex process reliant on the coordination of trans-acting enzymes to produce functional ribosomal subunits and secure the translational capacity of cells. The endoribonuclease (RNase) Las1 and the polynucleotide kinase (PNK) Grc3 assemble into a multienzyme complex, herein designated RNase PNK, to orchestrate processing of precursor ribosomal RNA (rRNA). RNase PNK belongs to the functionally diverse HEPN nuclease superfamily, whose members rely on distinct cues for nuclease activation. To establish how RNase PNK coordinates its dual enzymatic activities, we solved a series of cryo-EM structures of Chaetomium thermophilum RNase PNK in multiple conformational states. The structures reveal that RNase PNK adopts a butterfly-like architecture, harboring a composite HEPN nuclease active site flanked by discrete RNA kinase sites. We identify two molecular switches that coordinate nuclease and kinase function. Together, our structures and corresponding functional studies establish a new mechanism of HEPN nuclease activation essential for ribosome production.
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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.