RPL41

RPL41 (PF3D7_1144300) is a structural component of the 60S large subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, established through successive high-resolution cryo-EM and in situ cryo-electron tomography structures of the assembled ribosome (PMID:24913268, PMID:40825879). It is observed within the 60S subunit in structures of the free ribosome (PMID:24913268, PMID:26432834), in complex with the antimalarial (+)-mefloquine (PMID:28288098), and in native, actively translating ribosomes imaged inside infected erythrocytes (PMID:40825879). Beyond this membership in the assembled ribosomal complex, no specific enzymatic activity, binding partners, post-translational modifications, or individual functional role for RPL41 has been characterized in the available corpus.

1. 2014 Medium

   Whether RPL41 is a constituent of the P. falciparum cytoplasmic ribosome was resolved by placing it structurally within the assembled 80S particle.

   Evidence Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å, within which RPL41 is a 60S subunit component

   PMID:24913268

   Open questions at the time

   • No RPL41-specific function is assigned beyond structural presence
   • No individual binding partners or contacts of RPL41 are described
   • No perturbation or knockout of RPL41 to test its functional role
2. 2015 Medium

   Structural placement of RPL41 in the 60S subunit was reinforced across multiple ribosome states from blood-stage schizonts, confirming it is a stable constituent rather than a transient factor.

   Evidence Five sub-nanometer cryo-EM reconstructions with flexible-fitting atomic models of schizont-derived 80S ribosomes

   PMID:26432834

   Open questions at the time

   • No functional detail specific to RPL41 reported
   • Role of RPL41 in any translational state not distinguished
3. 2017 Medium

   RPL41 remains a resolved 60S component in the drug-bound ribosome, situating it within the pharmacologically targeted particle even though it is not itself implicated as the drug-binding site.

   Evidence Cryo-EM structure of the 80S ribosome at 3.2 Å bound to (+)-mefloquine, with binding-site residue mutagenesis

   PMID:28288098

   Open questions at the time

   • RPL41 is not shown to contribute to the mefloquine binding site
   • No functional consequence of drug binding attributed to RPL41
4. 2025 Medium

   Whether RPL41 is present in native, actively translating ribosomes in their cellular context was answered by resolving it in situ inside infected erythrocytes.

   Evidence Eight high-resolution in situ cryo-electron tomography structures of native translating 80S ribosomes inside P. falciparum-infected erythrocytes

   PMID:40825879

   Open questions at the time

   • No RPL41-specific mechanistic role in translation elongation established
   • No interactions unique to RPL41 resolved within translating states

• It remains unknown whether RPL41 has any function, binding partner, or phenotype beyond its structural membership in the 60S subunit.
• No genetic knockout or knockdown of RPL41
• No RPL41-specific binding partners or post-translational modifications identified
• No role in ribosome assembly, translational fidelity, or drug response demonstrated