ArticleRNA (New York, N.Y.)2019
Rrp5 establishes a checkpoint for 60S assembly during 40S maturation.
Article in RNA (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- ZNF574 is a quality control factor for defective ribosome biogenesis intermediates.Molecular cell · 2025Article
- The novel pre-rRNA detection workflow "Riboprobing" allows simple identification of undescribed RNA species.RNA (New York, N.Y.) · 2024Article
- A co-transcriptional ribosome assembly checkpoint controls nascent large ribosomal subunit maturation.Nature structural & molecular biology · 2023Article
- Quality control ensures fidelity in ribosome assembly and cellular health.The Journal of cell biology · 2023Review
- NOC1 is a direct MYC target, and its protein interactome dissects its activity in controlling nucleolar function.Frontiers in cell and developmental biology · 2023Article
- Reduction of nucleolar NOC1 leads to the accumulation of pre-rRNAs and induces Xrp1, affecting growth and resulting in cell competition.Journal of cell science · 2022Article
- Emergence of the primordial pre-60S from the 90S pre-ribosome.Cell reports · 2022Article
- Integrating Wheat Nucleolus Structure and Function: Variation in the Wheat Ribosomal RNA and Protein Genes.Frontiers in plant science · 2021Review
- snR30/U17 Small Nucleolar Ribonucleoprotein: A Critical Player during Ribosome Biogenesis.Cells · 2020Review
- A versatile cis-acting element reporter system to study the function, maturation and stability of ribosomal RNA mutants in archaea.Nucleic acids research · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Even though the RNAs contained in the small (40S) and large (60S) ribosomal subunits are cotranscribed, their assembly proceeds largely separately, involving entirely distinct machineries. Nevertheless, separation of the two subunits, an event that is critical for assembly of the small subunit, is delayed until domain I of the large subunit is transcribed, indicating crosstalk between the two assembly pathways. Here we show that this crosstalk is mediated by the assembly factor Rrp5, one of only three proteins required for assembly of both ribosomal subunits. Quantitative RNA binding and cleavage data demonstrate that early on, Rrp5 blocks separation of the two subunits, and thus 40S maturation by inhibiting the access of Rcl1 to promote cleavage of the nascent rRNA. Upon transcription of domain I of 25S rRNA, the 60S assembly factors Noc1/Noc2 bind both this RNA and Rrp5 to change the Rrp5 RNA binding mode to enable pre-40S rRNA processing. Mutants in the HEAT-repeat domain of Noc1 are deficient in the separation of the subunits, which is rescued by overexpression of wild-type but not inactive Rcl1 in vivo. Thus, Rrp5 establishes a checkpoint for 60S assembly during 40S maturation to ensure balanced levels of the two subunits.
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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.