ArticleMolecular and cellular biology2005
Esf2p, a U3-associated factor required for small-subunit processome assembly and compaction.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- The contribution and therapeutic implications of IGHMBP2 mutations on IGHMBP2 biochemical activity and ABT1 association.Biochimica et biophysica acta. Molecular basis of disease · 2024Article
- ABT1 modifies SMARD1 pathology via interactions with IGHMBP2 and stimulation of ATPase and helicase activity.JCI insight · 2023Article
- Maturation of the 90S pre-ribosome requires Mrd1 dependent U3 snoRNA and 35S pre-rRNA structural rearrangements.Nucleic acids research · 2018Article
- Article
- The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA.RNA (New York, N.Y.) · 2014Article
- Ribosome biogenesis in the yeast Saccharomyces cerevisiae.Genetics · 2013Review
- DExD/H-box RNA helicases in ribosome biogenesis.RNA biology · 2013Review
- The DEAD-box helicase eIF4A: paradigm or the odd one out?RNA biology · 2013Review
- New insights into the RNA-based mechanism of action of the anticancer drug 5'-fluorouracil in eukaryotic cells.PloS one · 2013Article
- In vivo approaches to dissecting the function of RNA helicases in eukaryotic ribosome assembly.Methods in enzymology · 2012Article
- Powering through ribosome assembly.RNA (New York, N.Y.) · 2009Review
- Mrd1p is required for release of base-paired U3 snoRNA within the preribosomal complex.Molecular and cellular biology · 2009Article
- Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery.Human molecular genetics · 2009Article
- Mrd1p binds to pre-rRNA early during transcription independent of U3 snoRNA and is required for compaction of the pre-rRNA into small subunit processomes.Nucleic acids research · 2008Article
- An improved, bias-reduced probabilistic functional gene network of baker's yeast, Saccharomyces cerevisiae.PloS one · 2007Article
- A survey of essential gene function in the yeast cell division cycle.Molecular biology of the cell · 2006Article
- The helicase Has1p is required for snoRNA release from pre-rRNA.Molecular and cellular biology · 2006Article
- The PINc domain protein Utp24, a putative nuclease, is required for the early cleavage steps in 18S rRNA maturation.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis.Nucleic acids research · 2006Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Esf2p is the Saccharomyces cerevisiae homolog of mouse ABT1, a protein previously identified as a putative partner of the TATA-element binding protein. However, large-scale studies have indicated that Esf2p is primarily localized to the nucleolus and that it physically associates with pre-rRNA processing factors. Here, we show that Esf2p-depleted cells are defective for pre-rRNA processing at the early nucleolar cleavage sites A0 through A2 and consequently are inhibited for 18S rRNA synthesis. Esf2p was stably associated with the 5' external transcribed spacer (ETS) and the box C+D snoRNA U3, as well as additional box C+D snoRNAs and proteins enriched within the small-subunit (SSU) processome/90S preribosomes. Esf2p colocalized on glycerol gradients with 90S preribosomes and slower migrating particles containing 5' ETS fragments. Strikingly, upon Esf2p depletion, chromatin spreads revealed that SSU processome assembly and compaction are inhibited and glycerol gradient analysis showed that U3 remains associated within 90S preribosomes. This suggests that in the absence of proper SSU processome assembly, early pre-rRNA processing is inhibited and U3 is not properly released from the 35S pre-rRNAs. The identification of ABT1 in a large-scale analysis of the human nucleolar proteome indicates that its role may also be conserved in mammals.
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