RPL3

PF3D7_1027800 (RPL3) is a structural constituent of the large (60S) subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, resolved within the large-subunit architecture by cryo-EM of the intact ribosome and confirmed in native, actively translating elongation complexes imaged in situ by cryo-electron tomography inside infected erythrocytes (PMID:24913268, PMID:40825879). Beyond its membership in the 60S subunit as a component of the native translational machinery, no mechanistic role specific to RPL3 — enzymatic activity, post-translational modification, or a defined functional interaction partner — has been characterized in the available corpus.

1. 2014 Medium

   Whether RPL3 is a bona fide constituent of the P. falciparum ribosome and where it sits was unknown until the intact 80S ribosome was resolved at near-atomic detail, placing RPL3 within the 60S subunit architecture.

   Evidence Cryo-EM structure of the P. falciparum 80S ribosome bound to emetine at 3.2 Å resolution

   PMID:24913268

   Open questions at the time

   • No functional experiment directed at RPL3 itself; role inferred solely from structural placement
   • No enzymatic activity, modification, or specific partner beyond the ribosome defined
   • Structure captured with a drug-bound ribosome, not a functional assay of RPL3
2. 2025 Medium

   Whether RPL3 occupies the same structural position in ribosomes that are actively translating within the parasite was addressed by imaging native ribosomes in situ, confirming RPL3 as a large-subunit component of elongation-state complexes inside the cell.

   Evidence In situ cryo-electron tomography with atomic-resolution modelling of native ribosomes inside P. falciparum-infected human erythrocytes

   PMID:40825879

   Open questions at the time

   • RPL3 role inferred from its presence in solved large-subunit models, not from an RPL3-directed experiment
   • No mechanistic contribution of RPL3 to translation elongation demonstrated
   • No RPL3-specific interactions distinguished from bulk ribosome architecture

• Whether RPL3 has any function beyond structural membership in the 60S subunit — a distinct enzymatic activity, regulatory role, post-translational modification, or specific non-ribosomal partner — remains uncharacterized in the available corpus.
• No functional or genetic assay targeting RPL3 in P. falciparum
• No defined interaction partner specific to RPL3
• No evidence for post-translational modification or regulatory activity of RPL3