ArticleMolecular and cellular biology2004
Npa1p, a component of very early pre-60S ribosomal particles, associates with a subset of small nucleolar RNPs required for peptidyl transferase center modification.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 81 citations in OpenAlex.
- Arabidopsis EMB2788/Npa1L1 is critical for pre-rRNA processing, ribosome biogenesis, and embryo development.The Plant journal : for cell and molecular biology · 2026Article
- A bifunctional H/ACA snoRNP mediates both pseudouridylation and rRNA scaffolding during ribosome assembly.bioRxiv : the preprint server for biology · 2026Article
- Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1.Nucleic acids research · 2026Article
- The snoRNP chaperone snR190 and the Npa1 complex form a macromolecular assembly required for 60S ribosomal subunit maturation.Nucleic acids research · 2025Article
- Article
- The DEAD-box protein Dbp6 is an ATPase and RNA annealase interacting with the peptidyl transferase center (PTC) of the ribosome.Nucleic acids research · 2023Article
- Rbp95 binds to 25S rRNA helix H95 and cooperates with the Npa1 complex during early pre-60S particle maturation.Nucleic acids research · 2022Article
- Synthetic negative genome screen of the GPN-loop GTPase NPA3 in Saccharomyces cerevisiae.Current genetics · 2022Article
- Emergence of the primordial pre-60S from the 90S pre-ribosome.Cell reports · 2022Article
- RNA folding and functions of RNA helicases in ribosome biogenesis.RNA biology · 2022Review
- The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly.Nature communications · 2021Article
- Association of snR190 snoRNA chaperone with early pre-60S particles is regulated by the RNA helicase Dbp7 in yeast.Nature communications · 2021Article
- Ribosome assembly factor URB1 contributes to colorectal cancer proliferation through transcriptional activation of ATF4.Cancer science · 2021Article
- RAPTOR promotes colorectal cancer proliferation by inducing mTORC1 and upregulating ribosome assembly factor URB1.Cancer medicine · 2020Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- The Npa1p complex chaperones the assembly of the earliest eukaryotic large ribosomal subunit precursor.PLoS genetics · 2018Article
- Turnover of aberrant pre-40S pre-ribosomal particles is initiated by a novel endonucleolytic decay pathway.Nucleic acids research · 2018Article
- Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.Nucleic acids research · 2017Article
- Disruption of ribosome assembly in yeast blocks cotranscriptional pre-rRNA processing and affects the global hierarchy of ribosome biogenesis.RNA (New York, N.Y.) · 2016Article
- Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly.Molecular and cellular biology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified a novel essential nucleolar factor required for the synthesis of 5.8S and 25S rRNAs termed Npa1p. In the absence of Npa1p, the pre-rRNA processing pathway leading to 5.8S and 25S rRNA production is perturbed such that the C2 cleavage within internal transcribed spacer 2 occurs prematurely. Npa1p accumulates in the immediate vicinity of the dense fibrillar component of the nucleolus and is predominantly associated with the 27SA2 pre-rRNA, the RNA component of the earliest pre-60S ribosomal particles. By mass spectrometry, we have identified the protein partners of Npa1p, which include eight putative helicases as well as the novel Npa2p factor. Strikingly, we also show that Npa1p can associate with a subset of H/ACA and C/D small nucleolar RNPs (snoRNPs) involved in the chemical modification of residues in the vicinity of the peptidyl transferase center. Our results suggest that 27SA2-containing pre-60S ribosomal particles are located at the interface between the dense fibrillar and the granular components of the nucleolus and that these particles can contain a subset of snoRNPs.
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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.