ArticleThe FEBS journal2012
The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells.
Article in The FEBS journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- Biophysical and Biochemical Assays for Screening Small Molecule Inhibitors Targeting Toxin-Ribosome Interactions.Toxins · 2026Review
- A fluorescence anisotropy-based competition assay to identify inhibitors against ricin and Shiga toxin ribosome interactions.Analytical biochemistry · 2024Article
- A Biparatopic Intrabody Renders Vero Cells Impervious to Ricin Intoxication.bioRxiv : the preprint server for biology · 2024Article
- Structure-based design and optimization of a new class of small molecule inhibitors targeting the P-stalk binding pocket of ricin.Bioorganic & medicinal chemistry · 2024Article
- Selective regulation in ribosome biogenesis and protein production for efficient viral translation.Archives of microbiology · 2021Review
- Small Molecule Inhibitors Targeting the Interaction of Ricin Toxin A Subunit with Ribosomes.ACS infectious diseases · 2020Article
- Introduction to theToxins · 2019Article
- Leucine 232 and hydrophobic residues at the ribosomal P stalk binding site are critical for biological activity of ricin.Bioscience reports · 2019Article
- RACK1 on and off the ribosome.RNA (New York, N.Y.) · 2019Article
- Review
- How Ricin Damages the Ribosome.Toxins · 2019Review
- Peptide Mimics of the Ribosomal P Stalk Inhibit the Activity of Ricin A Chain by Preventing Ribosome Binding.Toxins · 2018Article
- Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins.Toxins · 2018Review
- Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Scientific reports · 2017Article
- Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Scientific reports · 2017Article
- Structural insights into the interaction of the ribosomal P stalk protein P2 with a type II ribosome-inactivating protein ricin.Scientific reports · 2016Article
- Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.Toxicology and applied pharmacology · 2016Article
- Article
- The A1 Subunit of Shiga Toxin 2 Has Higher Affinity for Ribosomes and Higher Catalytic Activity than the A1 Subunit of Shiga Toxin 1.Infection and immunity · 2016Article
- Do the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Toxins · 2015Review
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
Ricin A-chain (RTA) depurinates the sarcin-ricin loop of 28S ribosomal RNA and inhibits protein synthesis in mammalian cells. In yeast, the ribosomal stalk facilitates the interaction of RTA with the ribosome and subsequent depurination. Despite homology between the stalk structures from yeast and humans, there are notable differences. The human ribosomal stalk contains two identical heterodimers of P1 and P2 bound to P0, whereas the yeast stalk consists of two different heterodimers, P1α-P2β and P2α-P1β, bound to P0. RTA exhibits higher activity towards mammalian ribosomes than towards ribosomes from other organisms, suggesting that the mode of interaction with ribosomes may vary. Here, we examined whether the human ribosomal stalk proteins facilitate the interaction of RTA with human ribosomes and subsequent depurination of the sarcin-ricin loop. Using small interfering RNA-mediated knockdown of P1/P2 expression in human cells, we demonstrated that the depurination activity of RTA is lower when P1 and P2 levels are reduced. Biacore analysis showed that ribosomes from P1/P2-depleted cells have a reduced ability to bind RTA, which correlates with reduced depurination activity both in vitro and inside cells. RTA interacts directly with recombinant human P1-P2 dimer, further demonstrating the importance of human P1 and P2 in enabling RTA to bind and depurinate human ribosomes.
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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.