RPL38

PF3D7_1130100 (RPL38) is a structural component of the 60S large subunit of the P. falciparum 80S cytoplasmic ribosome, identified as a constituent of the intact ribosomal complex by successive high-resolution cryo-EM structures of the parasite ribosome (PMID:24913268, PMID:26432834). It has been resolved within the 80S ribosome in complexes bound to translation-inhibiting ligands such as emetine and mefloquine (PMID:24913268, PMID:28288098), and within the physiologically active, translating ribosome imaged in situ inside infected erythrocytes by cryo-electron tomography (PMID:40825879). Beyond its membership in the 60S subunit as established by these structural studies, no RPL38-specific enzymatic activity, binding partners, post-translational modifications, or individual functional role has been characterized in the available corpus.

1. 2014 Medium

   Whether RPL38 is a resolvable structural constituent of the P. falciparum ribosome was first addressed by placing it within the atomic architecture of the 80S complex.

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

   PMID:24913268

   Open questions at the time

   • No RPL38-specific function or activity established beyond 60S subunit membership
   • No binding partners or post-translational modifications identified
   • Contribution of RPL38 to translation or ribosome assembly not tested
2. 2015 Medium

   Multiple independent reconstructions from blood-stage schizonts confirmed RPL38 as a consistent structural constituent of the 60S subunit rather than a variably occupied position.

   Evidence Five cryo-EM reconstructions with flexible-fitting atomic model building from schizont-purified ribosomes

   PMID:26432834

   Open questions at the time

   • Does not address RPL38's individual role in subunit assembly or function
   • No stage-specific or condition-dependent behavior of RPL38 examined
3. 2017 Medium

   Structural placement of RPL38 was reaffirmed in a ribosome captured with an antimalarial ligand at the GTPase-associated centre, situating the protein within the translationally competent particle.

   Evidence Cryo-EM at 3.2 Å with mefloquine bound and mutagenesis of binding-site residues

   PMID:28288098

   Open questions at the time

   • Mutagenesis targeted the drug-binding site, not RPL38 itself
   • No direct link between RPL38 and the ligand-binding or catalytic function shown
4. 2025 Medium

   Whether the structural assignment holds in the native cellular context, rather than in purified particles, was resolved by imaging actively translating ribosomes in situ.

   Evidence In situ cryo-electron tomography inside infected erythrocytes yielding eight structures of the native translating ribosome

   PMID:40825879

   Open questions at the time

   • Confirms native complex membership but assigns no RPL38-specific mechanistic role
   • No functional perturbation of RPL38 tested in the native context

• It remains unknown whether RPL38 has any function specific to itself beyond serving as a structural building block of the 60S subunit.
• No genetic knockdown/knockout phenotype for RPL38 reported
• No RPL38-specific binding partners or extraribosomal roles characterized
• No post-translational modifications or regulatory features identified