Affinage · Plasmodium

RPS27

PF3D7_1308300 · 40S ribosomal protein S27

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RPS27 (PF3D7_1308300) is a constituent protein of the 40S small subunit of the Plasmodium falciparum 80S ribosome, resolved as part of the assembled particle by successive cryo-EM and in situ cryo-electron tomography studies (PMID:24913268, PMID:40825879). It is present within the small subunit architecture visualized in the intact ribosome, including native, actively translating ribosomes captured inside infected erythrocytes and states that differentiate the malarial ribosome from its mammalian counterpart (PMID:26432834, PMID:40825879). Beyond this structural membership in the 80S ribosome, the specific molecular function, interactions, and post-translational modifications of RPS27 itself have not been individually interrogated in the available corpus; every finding derives from whole-ribosome structural work in which RPS27 was not separately mutated or functionally dissected.

Mechanistic history

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

    Establishing the first high-resolution structure of the intact malarial ribosome placed the 40S small subunit — and therefore RPS27 as one of its component proteins — in defined structural context and showed how a translation inhibitor engages the small subunit.

    Evidence Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome bound to emetine, which occupies the small-subunit E-site to block translocation

    PMID:24913268

    Open questions at the time
    • RPS27 is only implicitly part of the small subunit and is not individually interrogated or mutagenized
    • No RPS27-specific function, contact, or dynamics resolved
    • Single study
  2. 2015 Medium

    Capturing multiple translational states of the blood-stage ribosome defined dynamic features of the 40S subunit that distinguish the parasite ribosome from the mammalian one, refining the structural environment in which RPS27 sits.

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

    PMID:26432834

    Open questions at the time
    • RPS27 is not individually interrogated within the small subunit
    • No functional role attributed specifically to RPS27
    • Single lab study
  3. 2025 Medium

    Resolving native, actively translating ribosomes in situ established the molecular architecture of the malarial elongation cycle and confirmed RPS27 as a structural component of the 40S subunit in physiologically translating complexes rather than only purified particles.

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

    PMID:40825879

    Open questions at the time
    • RPS27 itself is not individually mutated or functionally dissected
    • No RPS27-specific interactions or modifications resolved
    • Single study

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether RPS27 has any function, interaction, or regulatory role independent of its structural incorporation into the 40S subunit remains entirely unaddressed.
  • No genetic knockout, knockdown, or complementation of RPS27
  • No assembly, extra-ribosomal, or post-translational modification data specific to RPS27
  • No direct interaction partners established beyond ribosome membership

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
40S ribosomal small subunitP. falciparum 80S 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 the small (40S) subunit, within which RPS27 (PF3D7_1308300) is a constituent protein; the structure established that emetine binds the E-site of the small subunit to block mRNA/tRNA translocation. Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine eLife Medium 24913268
2015 Five cryo-EM reconstructions of P. falciparum blood-stage schizont ribosomes at sub-nanometer resolution, with atomic models built by flexible fitting, established structural and dynamic features of the 80S ribosome (including the 40S small subunit where RPS27/PF3D7_1308300 resides) that differentiate it from mammalian ribosomes. Cryo-EM with flexible-fitting atomic model building from blood-stage schizont ribosomes; five reconstructions capturing different translational states Nucleic acids research Medium 26432834
2025 Eight high-resolution in situ cryo-electron tomography structures of the native P. falciparum ribosome in actively translating states inside infected erythrocytes were determined, establishing the molecular architecture of the malarial translation elongation cycle; RPS27/PF3D7_1308300 is a structural component of the 40S small subunit visible in these native complexes. In situ cryo-electron tomography at high resolution inside P. falciparum-infected human erythrocytes; eight structures of actively translating ribosomes Nature structural & molecular biology Medium 40825879

Source papers

Stage 0 corpus · 4 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 276 24913268
2015 Dynamical features of the Plasmodium falciparum ribosome during translation. Nucleic acids research 46 26432834
2025 Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug. Nature structural & molecular biology 10 40825879
2025 Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Structure (London, England : 1993) 4 40480224