ArticleNucleic acids research2013
Solution structure of human P1•P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Structure of Ribosome-Inactivating Protein fromToxins · 2025Article
- Fragment Screening to Identify Inhibitors Targeting Ribosome Binding of Shiga Toxin 2.ACS infectious diseases · 2024Article
- Structure-Function Analysis of the A1 Subunit of Shiga Toxin 2 with Peptides That Target the P-Stalk Binding Site and Inhibit Activity.Biochemistry · 2024Article
- Simultaneous measurement of nascent transcriptome and translatome using 4-thiouridine metabolic RNA labeling and translating ribosome affinity purification.Nucleic acids research · 2023Article
- The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.Nucleic acids research · 2022Article
- A Sixty-Year Research and Development of Trichosanthin, a Ribosome-Inactivating Protein.Toxins · 2022Review
- Linear Epitope Binding Patterns of Grass Pollen-Specific Antibodies in Allergy and in Response to Allergen-Specific Immunotherapy.Frontiers in allergy · 2022Article
- Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural basis for the interaction of Shiga toxin 2a with a C-terminal peptide of ribosomal P stalk proteins.The Journal of biological chemistry · 2020Article
- Peptide Mimics of the Ribosomal P Stalk Inhibit the Activity of Ricin A Chain by Preventing Ribosome Binding.Toxins · 2018Article
- The ribosomal stalk protein is crucial for the action of the conserved ATPase ABCE1.Nucleic acids research · 2018Article
- Review
- The Interaction between the Ribosomal Stalk Proteins and Translation Initiation Factor 5B Promotes Translation Initiation.Molecular and cellular biology · 2018Article
- Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins.Toxins · 2018Review
- The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.Nucleic acids research · 2018Article
- 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
- Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.Molecules (Basel, Switzerland) · 2016Review
- Article
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10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lateral ribosomal stalk is responsible for binding and recruiting translation factors during protein synthesis. The eukaryotic stalk consists of one P0 protein with two copies of P1•P2 heterodimers to form a P0(P1•P2)₂ pentameric P-complex. Here, we have solved the structure of full-length P1•P2 by nuclear magnetic resonance spectroscopy. P1 and P2 dimerize via their helical N-terminal domains, whereas the C-terminal tails of P1•P2 are unstructured and can extend up to ∼125 Å away from the dimerization domains. (15)N relaxation study reveals that the C-terminal tails are flexible, having a much faster internal mobility than the N-terminal domains. Replacement of prokaryotic L10(L7/L12)₄/L11 by eukaryotic P0(P1•P2)₂/eL12 rendered Escherichia coli ribosome, which is insensitive to trichosanthin (TCS), susceptible to depurination by TCS and the C-terminal tail was found to be responsible for this depurination. Truncation and insertion studies showed that depurination of hybrid ribosome is dependent on the length of the proline-alanine rich hinge region within the C-terminal tail. All together, we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS.
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