PF3D7_1460700

PF3D7_1460700 (L27) is a constituent ribosomal protein of the 60S large subunit of the Plasmodium falciparum 80S cytoplasmic ribosome, resolved as part of the native parasite ribosome complex by cryo-EM at 3.2 Å resolution (PMID:24913268) and localized within the 60S subunit of actively translating ribosomes by in situ cryo-electron tomography inside infected erythrocytes (PMID:40825879). Beyond its membership in the 60S subunit of the ribosome, no function, interaction partner, or mechanism specific to L27 itself has been characterized in the available corpus.

1. 2014 Medium

   Whether L27 is a bona fide component of the parasite ribosome and where it sits structurally was addressed by resolving the intact P. falciparum 80S ribosome, establishing L27 as a 60S subunit constituent.

   Evidence Cryo-electron microscopy of the P. falciparum 80S ribosome at 3.2 Å resolution

   PMID:24913268

   Open questions at the time

   • No function or activity specific to L27 distinguished from bulk ribosome structure
   • No interaction partners or regulatory role for L27 individually established
   • Structure of purified complex, not in a cellular translation context
2. 2025 Medium

   Whether L27's structural placement holds in the physiological, translating ribosome was addressed by in-cell structural biology, confirming L27 within the 60S subunit of natively translating malarial ribosomes.

   Evidence In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes, yielding eight structures of the elongating ribosome

   PMID:40825879

   Open questions at the time

   • No L27-specific functional contribution to translation elongation defined
   • No evidence for any role of L27 outside the ribosome complex
   • Single study; no perturbation of L27 to test its requirement

• It remains unknown whether L27 has any function, interaction, or phenotype distinct from its structural membership in the 60S subunit.
• No genetic knockdown/knockout of L27 to assess essentiality
• No biochemical or interaction data specific to L27
• No evidence of extraribosomal roles