ArticleMolecular and cellular biology1997
Fal1p is an essential DEAD-box protein involved in 40S-ribosomal-subunit biogenesis in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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102 citing papers in PubMed, 162 citations in OpenAlex.
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- The Terminal Extensions of Dbp7 Influence Growth and 60S Ribosomal Subunit Biogenesis inInternational journal of molecular sciences · 2023Article
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- A functional connection between translation elongation and protein folding at the ribosome exit tunnel in Saccharomyces cerevisiae.Nucleic acids research · 2021Article
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- Prefoldin-like Bud27 influences the transcription of ribosomal components and ribosome biogenesis inRNA (New York, N.Y.) · 2020Article
- Role of the 40S beak ribosomal protein eS12 in ribosome biogenesis and function inRNA biology · 2020Article
- An Interaction Network of RNA-Binding Proteins Involved inMolecular & cellular proteomics : MCP · 2020Article
- The ribotoxin α-sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes.Nucleic acids research · 2020Article
- Sgd1 is an MIF4G domain-containing cofactor of the RNA helicase Fal1 and associates with the 5' domain of the 18S rRNA sequence.RNA biology · 2020Article
- USP16 counteracts mono-ubiquitination of RPS27a and promotes maturation of the 40S ribosomal subunit.eLife · 2020Article
- The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 inCells · 2019Article
- Impact of intron removal from tRNA genes on Saccharomyces cerevisiae.Nucleic acids research · 2019Article
42 more citing papers are in PubMed but not listed here.
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A previously uncharacterized Saccharomyces cerevisiae gene, FAL1, was found by sequence comparison as a homolog of the eukaryotic translation initiation factor 4A (eIF4A). Fal1p has 55% identity and 73% similarity on the amino acid level to yeast eIF4A, the prototype of ATP-dependent RNA helicases of the DEAD-box protein family. Although clearly grouped in the eIF4A subfamily, the essential Fal1p displays a different subcellular function and localization. An HA epitope-tagged Fal1p is localized predominantly in the nucleolus. Polysome analyses in a temperature-sensitive fal1-1 mutant and a Fal1p-depleted strain reveal a decrease in the number of 40S ribosomal subunits. Furthermore, these strains are hypersensitive to the aminoglycoside antibiotics paromomycin and neomycin. Pulse-chase labeling of pre-rRNA and steady-state-level analysis of pre-rRNAs and mature rRNAs by Northern hybridization and primer extension in the Fal1p-depleted strain show that Fal1p is required for pre-rRNA processing at sites A0, A1, and A2. Consequently, depletion of Fal1p leads to decreased 18S rRNA levels and to an overall deficit in 40S ribosomal subunits. Together, these results implicate Fal1p in the 18S rRNA maturation pathway rather than in translation initiation.
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