Affinage · Plasmodium

MED17

PF3D7_0520200 · mediator of RNA polymerase II transcription subunit 17, putative

Annotated
2026-09-08
4 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0520200 (MED17) is a subunit of the Plasmodium falciparum Mediator complex, the coactivator module associated with RNA polymerase II transcription (PMID:35557691). It was physically identified as an interaction partner of the conserved Mediator subunit PfMed31 by reciprocal coimmunoprecipitation and mass spectrometry, establishing its membership in the P. falciparum Mediator complex, with the head-module MED17 implicated in bridging the head and middle modules via a Med17–Med21 interaction conserved from yeast (PMID:35557691). Beyond its complex membership, no direct enzymatic activity, structure, or dedicated functional characterization of MED17 itself has been established in the available corpus; its only additional appearance is as one member of the PfSET10 nuclear interaction network during blood-stage development (PMID:39445823).

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2022 Medium

    Whether P. falciparum encodes a functional Mediator complex and which subunits associate was unresolved; identifying MED17 as a PfMed31 partner established that PF3D7_0520200 is a bona fide Mediator subunit rather than a merely annotated ortholog.

    Evidence Reciprocal coimmunoprecipitation of PfMed31 followed by mass spectrometry in P. falciparum

    PMID:35557691

    Open questions at the time
    • Single lab, single method; no reciprocal Co-IP starting from MED17 itself
    • The proposed Med17-Med21 head-to-middle bridging role is inferred from yeast conservation, not directly demonstrated in P. falciparum
    • No functional consequence of MED17 loss on transcription was tested
  2. 2024 Low

    Whether MED17 participates in chromatin-associated regulatory networks beyond core Mediator was unknown; proximity labeling placed it in the PfSET10 nuclear network during intraerythrocytic development.

    Evidence TurboID proximity labeling coupled with mass spectrometry in P. falciparum blood stages

    PMID:39445823

    Open questions at the time
    • Proximity labeling reflects spatial neighborhood, not direct interaction; MED17 is one of many listed interactors with no MED17-specific follow-up
    • No evidence that MED17 is functionally required for PfSET10 activity or vice versa
    • Stage- and locus-specificity of any MED17 role remains uncharacterized

Open questions

Synthesis pass · forward-looking unresolved questions
  • The direct molecular function of MED17, its structural role within the Mediator complex, and any phenotype from its perturbation in P. falciparum remain unestablished.
  • No genetic knockdown/knockout of MED17 to define its contribution to RNA Pol II transcription
  • No structural or biochemical validation of the head-to-middle module bridging role in P. falciparum
  • No target genes or transcriptional programs assigned to MED17

Mechanism profile

Synthesis pass · controlled-vocabulary classification

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2022 PF3D7_0520200 (MED17/PfMed17) was physically identified as an interaction partner of the conserved Mediator subunit PfMed31 by coimmunoprecipitation and mass spectrometry, establishing its membership in the P. falciparum Mediator complex. The body text notes that MED17 (head module) connects the head and middle modules via a Med17–Med21 interaction conserved from yeast. Coimmunoprecipitation (Co-IP) of PfMed31 followed by mass spectrometry ACS omega Medium 35557691
2024 PF3D7_0520200 (MED17) was identified as part of the PfSET10 nuclear interaction network (mediators of RNA polymerase II) via TurboID proximity labeling coupled with mass spectrometry, placing it in a chromatin modulation network active during P. falciparum blood-stage intraerythrocytic development. TurboID proximity labeling coupled with mass spectrometry mSphere Low 39445823

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1968 DNA, RNA , and protein synthesis in erythrocytic forms of Plasmodium knowlesi. The American journal of tropical medicine and hygiene 56 4971014
2019 Protein-RNA interactions important for Plasmodium transmission. PLoS pathogens 16 31877193
2024 The Plasmodium falciparum histone methyltransferase SET10 participates in a chromatin modulation network crucial for intraerythrocytic development. mSphere 0 39445823
2022 Mediator Complex of the Malaria Parasite Plasmodium falciparum Associates with Evolutionarily Novel Subunits. ACS omega 0 35557691