Affinage · Plasmodium

PF3D7_1309100

60S ribosomal protein L24, putative

Annotated
2026-09-08
5 papers in source corpus 3 papers cited in narrative 3 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1309100 (L24) is a structural component of the 60S large subunit of the Plasmodium falciparum 80S cytoplasmic ribosome, resolved as part of the assembled translation machinery in successive cryo-EM structures of the malarial ribosome (PMID:24913268, PMID:26432834). In situ cryo-electron tomography inside P. falciparum-infected erythrocytes confirms L24 as a 60S component of the native ribosome captured in actively translating states (PMID:40825879). Beyond this membership in the assembled 80S ribosome, no experiment in the available corpus assigns L24 a specific catalytic, binding, or regulatory function distinct from the ribosome as a whole; its individual mechanistic role has not been characterized.

Mechanistic history

Synthesis pass · year-by-year structured walk · 3 steps
  1. 2014 Low

    Establishing whether L24 is part of the assembled malarial ribosome required a structure of the P. falciparum 80S particle, which placed L24 within the 60S large subunit.

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

    PMID:24913268

    Open questions at the time
    • structural membership does not assign L24 a specific catalytic, binding, or regulatory function
    • no experiment probed L24 individually
    • no direct interaction partners of L24 mapped beyond the ribosome context
  2. 2015 Low

    Confirming L24 is present during active translation extended the static structural placement by resolving its position in ribosomes purified from blood-stage schizonts.

    Evidence Cryo-EM reconstruction with flexible-fitting atomic model building of ribosomes from P. falciparum blood-stage schizonts

    PMID:26432834

    Open questions at the time
    • membership in the translating ribosome does not reveal a stage-specific or L24-specific function
    • no functional perturbation of L24 performed
    • contribution of L24 to subunit assembly or stability untested
  3. 2025 Low

    Determining whether L24's placement holds in the native cellular environment was addressed by in situ tomography, confirming L24 as a 60S component of ribosomes actively translating inside infected erythrocytes.

    Evidence In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes yielding eight structures of actively translating ribosomes

    PMID:40825879

    Open questions at the time
    • native structural confirmation still does not define an L24-specific mechanistic role
    • no genetic or biochemical dissection of L24 function
    • no assignment of L24-specific interactions with mRNA, tRNA, or translation factors

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether L24 has any function beyond being a constituent of the 60S subunit — a role in ribosome assembly, translational regulation, or stage-specific translation — remains unaddressed in the available corpus.
  • no loss-of-function or knockdown study of L24
  • no biochemical characterization of L24-specific binding partners or activity
  • no evidence distinguishing L24's contribution from that of the ribosome as a whole

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
60S large ribosomal subunit of the P. falciparum 80S cytoplasmic ribosome

Evidence

Reading pass · 3 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2014 Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the structural context of L24 (PF3D7_1309100) as a component of the 60S large subunit within the cytoplasmic ribosome; the structure establishes L24's membership in the assembled 80S complex but does not assign a specific mechanistic role to L24 beyond this membership. Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome eLife Low 24913268
2015 Cryo-EM reconstructions of P. falciparum blood-stage schizont ribosomes at sub-nanometer resolution with atomic model building confirmed the presence and structural position of 60S subunit proteins including L24 (PF3D7_1309100) within the 80S ribosome during translation, establishing its membership in the translating ribosome. Cryo-EM reconstruction with flexible-fitting atomic model building of ribosomes purified from P. falciparum blood-stage schizonts Nucleic acids research Low 26432834
2025 In situ cryo-electron tomography of P. falciparum-infected erythrocytes determined eight high-resolution structures of the native malarial ribosome in actively translating states, confirming L24 (PF3D7_1309100) as a structural component of the 60S subunit within the native cellular translation machinery; no specific mechanistic role for L24 beyond complex membership was established. In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes Nature structural & molecular biology Low 40825879

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. eLife 272 24913268
2017 Mefloquine targets the Plasmodium falciparum 80S ribosome to inhibit protein synthesis. Nature microbiology 136 28288098
2015 Dynamical features of the Plasmodium falciparum ribosome during translation. Nucleic acids research 45 26432834
2025 Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug. Nature structural & molecular biology 7 40825879
2025 Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Structure (London, England : 1993) 3 40480224