Affinage · Plasmodium

RAD23

PF3D7_1011700 · DNA repair protein RAD23, 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_1011700 (RAD23) is a putative P. falciparum DNA repair protein placed within the parasite's excision repair response to genotoxic stress: in the mutator strains Dd2 and W2, which fail to mount a DNA repair transcriptional response after MMS-induced damage, RAD23 was one of 18 DNA repair genes found to carry point mutations (PMID:27033103). It has additionally been named as a component of the parasite ubiquitin-proteasome system alongside Dsk2 and Ddi1, linked to the unfolded protein response under stress (PMID:40113723). No direct biochemical, structural, or functional experiment has been performed on PF3D7_1011700 itself in the available corpus; both findings mention it as a member of a gene set or complex rather than characterizing its mechanism, so beyond these associations its molecular activity, partners, and role are uncharacterized.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2016 Low

    To locate RAD23 within the parasite's genotoxic stress response, transcriptional and genomic profiling of MMS-treated mutator strains tested which DNA repair genes are compromised when repair induction fails.

    Evidence Genome-wide transcriptional profiling after MMS treatment plus genome sequencing of Dd2 and W2 mutator strains

    PMID:27033103

    Open questions at the time
    • RAD23 is one of 18 listed genes with no individual functional assay specific to it
    • point mutations were not shown to alter RAD23 function or repair activity
    • no direct evidence that RAD23 participates in excision repair mechanistically
  2. 2025 Low

    To situate RAD23 in the parasite proteostasis network, a study of PfDdi1 named RAD23 as a co-member of the ubiquitin-proteasome system tied to the unfolded protein response.

    Evidence Computational docking and molecular dynamics simulation focused on PfDdi1, with RAD23 cited contextually as a UPS component alongside Dsk2 and Ddi1

    PMID:40113723

    Open questions at the time
    • no experiment was performed on RAD23 itself in this study
    • physical interaction of RAD23 with Dsk2, Ddi1, or the proteasome not demonstrated
    • role of RAD23 in the unfolded protein response not directly tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether PF3D7_1011700 has any direct biochemical activity, binding partners, or defined role in either DNA repair or the ubiquitin-proteasome system remains entirely uncharacterized.
  • no direct enzymatic or binding assay on RAD23
  • no structural model specific to RAD23
  • no genetic knockout or complementation defining its cellular role

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
2016 RAD23 (PF3D7_1011700) is among 18 DNA repair genes found to carry point mutations in two P. falciparum mutator strains (Dd2 and W2) that fail to induce DNA repair upon MMS-induced DNA damage, placing RAD23 within the excision repair system transcriptionally regulated in response to genotoxic stress. Genome-wide transcriptional profiling after MMS treatment combined with genome sequencing of mutator strains to identify point mutations in DNA repair genes Scientific reports Low 27033103
2025 RAD23 (PF3D7_1011700) is identified as a component of the P. falciparum ubiquitin-proteasome system (UPS) alongside Dsk2 and Ddi1, implicated in the unfolded protein response under stress; however, the paper's experimental work focuses on PfDdi1, not RAD23 directly. Computational docking and molecular dynamics simulation (study of PfDdi1, with RAD23 mentioned as a UPS component) Cell biochemistry and biophysics Low 40113723

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2016 DNA damage regulation and its role in drug-related phenotypes in the malaria parasites. Scientific reports 56 27033103
2005 DNA-[adenine] methylation in lower eukaryotes. Biochemistry. Biokhimiia 42 15948708
1987 From Laveran's discovery to DNA probes: new trends in diagnosis of malaria. Lancet (London, England) 31 2892060
2025 Computational Analysis of Plasmodium falciparum DNA Damage Inducible Protein 1 (PfDdi1): Insights into Binding of Artemisinin and its Derivatives and Implications for Antimalarial Drug Design. Cell biochemistry and biophysics 4 40113723