RPS26

PF3D7_0217800 (RPS26) is a component of the small (40S) subunit of the P. falciparum 80S ribosome, within which it has been visualized structurally but not individually characterized (PMID:24913268, PMID:26432834, PMID:40825879). High-resolution cryo-EM of the blood-stage ribosome placed RPS26 in its structural context within the 40S subunit and defined features distinguishing the malarial ribosome from its mammalian counterpart (PMID:24913268, PMID:26432834), and in situ cryo-ET of native, actively translating ribosomes inside infected erythrocytes confirmed its presence in functional 40S complexes engaged in the translation elongation cycle (PMID:40825879). Beyond its membership in the 40S subunit, no experiment in the available corpus has directly characterized the specific molecular function, interactions, or post-translational modifications of RPS26 itself.

1. 2014 Medium

   Establishing the atomic architecture of the P. falciparum small ribosomal subunit was needed to place RPS26 in structural context; the first high-resolution cryo-EM structure of the 80S ribosome accomplished this and localized the drug-binding site on the small subunit.

   Evidence Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome–emetine complex

   PMID:24913268

   Open questions at the time

   • RPS26 is resolved only as part of the 40S subunit; its individual function is not tested
   • No RPS26-specific interactions or modifications are addressed
   • Single conformational state captured with a bound inhibitor
2. 2015 Medium

   Whether the malarial ribosome adopts multiple conformational states and differs structurally from the mammalian ribosome was addressed by multiple cryo-EM reconstructions, reinforcing the structural context in which RPS26 sits as a 40S component.

   Evidence Cryo-EM with flexible fitting across multiple ribosome conformational states from P. falciparum blood-stage schizonts

   PMID:26432834

   Open questions at the time

   • Findings pertain to the ribosome as a whole, not RPS26 individually
   • No functional perturbation of RPS26 performed
   • Dynamics of RPS26 relative to the rest of the 40S not isolated
3. 2025 Medium

   Whether the ribosome, and thus RPS26, could be observed in native translating states in situ was resolved by high-resolution cryo-ET inside infected erythrocytes, confirming RPS26's presence in actively elongating 40S complexes and revealing drug-induced shifts toward ribosome biogenesis.

   Evidence In situ cryo-ET at high resolution inside P. falciparum-infected human erythrocytes with translation-inhibitor perturbation

   PMID:40825879

   Open questions at the time

   • RPS26 is inferred from 40S membership, not directly characterized
   • No RPS26-specific role in elongation or biogenesis demonstrated
   • Interactions and modifications of RPS26 remain undefined

• The specific molecular function, binding partners beyond the 40S subunit, and any post-translational modifications of RPS26 (PF3D7_0217800) itself remain uncharacterized in the available corpus.
• No experiment isolates RPS26's individual contribution to translation
• No RPS26-specific interactome or modification data
• No genetic perturbation of RPS26 in P. falciparum reported