ArticlePloS one2009
Clusters of basic amino acids contribute to RNA binding and nucleolar localization of ribosomal protein L22.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Ribosomal protein control of hematopoietic stem cell transformation through regulation of metabolism.Cell reports · 2025Article
- Ribosomal RNA transcription regulates splicing through ribosomal protein RPL22.Cell chemical biology · 2025Article
- CRISPR screening uncovers nucleolar RPL22 as a heterochromatin destabilizer and senescence driver.Nucleic acids research · 2024Article
- Targeting of Hmo1 to subcompartments of the budding yeast nucleolus.Molecular biology of the cell · 2023Article
- RNA-binding is an ancient trait of the Annexin family.Frontiers in cell and developmental biology · 2023Article
- Tissue-specific expression of ribosomal protein paralogue eRpL22-like in Drosophila melanogaster eye development.Developmental dynamics : an official publication of the American Association of Anatomists · 2020Article
- Specialized eRpL22 paralogue-specific ribosomes regulate specific mRNA translation in spermatogenesis inMolecular biology of the cell · 2019Article
- Review
- Introns provide a platform for intergenic regulatory feedback of RPL22 paralogs in yeast.PloS one · 2018Article
- Regulatory Roles of Rpl22 in Hematopoiesis: An Old Dog with New Tricks.Critical reviews in immunology · 2015Review
- Genes of the RNASE5 pathway contain SNP associated with milk production traits in dairy cattle.Genetics, selection, evolution : GSE · 2013Article
- Charge versus sequence for nuclear/nucleolar localization of plant ribosomal proteins.Plant molecular biology · 2013Article
- The folded and disordered domains of human ribosomal protein SA have both idiosyncratic and shared functions as membrane receptors.Bioscience reports · 2012Article
- Expression of ribosomal protein L22e family members in Drosophila melanogaster: rpL22-like is differentially expressed and alternatively spliced.Nucleic acids research · 2011Article
- Growth-promoting properties of Epstein-Barr virus EBER-1 RNA correlate with ribosomal protein L22 binding.Journal of virology · 2009Article
- RpL22e, but not RpL22e-like-PA, is SUMOylated and localizes to the nucleoplasm of Drosophila meiotic spermatocytes.Nucleus (Austin, Tex.)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The ribosomal protein L22 is a component of the 60S eukaryotic ribosomal subunit. As an RNA-binding protein, it has been shown to interact with both cellular and viral RNAs including 28S rRNA and the Epstein-Barr virus encoded RNA, EBER-1. L22 is localized to the cell nucleus where it accumulates in nucleoli. Although previous studies demonstrated that a specific amino acid sequence is required for nucleolar localization, the RNA-binding domain has not been identified. Here, we investigated the hypothesis that the nucleolar accumulation of L22 is linked to its ability to bind RNA. To address this hypothesis, mutated L22 proteins were generated to assess the contribution of specific amino acids to RNA binding and protein localization. Using RNA-protein binding assays, we demonstrate that basic amino acids 80-93 are required for high affinity binding of 28S rRNA and EBER-1 by L22. Fluorescence localization studies using GFP-tagged mutated L22 proteins further reveal that basic amino acids 80-93 are critical for nucleolar accumulation and for incorporation into ribosomes. Our data support the growing consensus that the nucleolar accumulation of ribosomal proteins may not be mediated by a defined localization signal, but rather by specific interaction with established nucleolar components such as rRNA.
Indexed as
Identifiers
What OpenQuestion holds
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.