Affinage · Plasmodium

NOP5

PF3D7_1008800 · nucleolar protein 5, putative

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NOP5 (PF3D7_1008800) is a putative nucleolar protein of Plasmodium falciparum whose function has not been directly characterized in the available corpus. It was detected in the parasite nuclear proteome by high-accuracy mass spectrometry and is noted as one of only three proteins previously localized to the parasite nucleolus (PMID:23181666). In DNA oligonucleotide pull-downs using probes bearing the de novo regulatory motif 028, NOP5 co-enriched with the transcription factor AP2-I and chromatin-associated factors (bromodomain proteins, HMGB3, and a SWIB/MDM2 domain protein), placing it in physical association with a regulatory DNA motif complex during intraerythrocytic stages (PMID:29649445). Beyond this nucleolar localization and pull-down association, no enzymatic activity, structure, direct binding partner, or functional mechanism has been established for NOP5 itself in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2012 Low

    Establishing where NOP5 resides, mass spectrometry of isolated nuclei placed it in the P. falciparum nuclear proteome and flagged its prior nucleolar localization, giving a first subcellular anchor for an otherwise uncharacterized protein.

    Evidence Organellar proteomics by high-accuracy mass spectrometry of isolated parasite nuclei

    PMID:23181666

    Open questions at the time
    • Detection in a pan-nuclear catalog only; no functional experiment performed on NOP5 itself
    • No enzymatic activity or molecular role assigned
    • Nucleolar assignment cited from prior work rather than demonstrated in this study
  2. 2018 Low

    Asking what NOP5 associates with, DNA pull-downs showed it co-enriches with AP2-I and chromatin factors on a specific regulatory motif, providing the first (associative) link between this nucleolar protein and a transcriptional regulatory complex.

    Evidence DNA oligonucleotide pull-down with regulatory motif 028 probe followed by mass spectrometry, intraerythrocytic stages

    PMID:29649445

    Open questions at the time
    • Single large-scale pull-down without functional follow-up specific to NOP5
    • Association may be indirect; no reciprocal or direct binding validation for NOP5
    • No demonstration that NOP5 contributes to regulatory activity of the motif complex

Open questions

Synthesis pass · forward-looking unresolved questions
  • The direct molecular activity of NOP5, its role in nucleolar biology, and whether its association with the AP2-I regulatory motif complex is functional or incidental remain unknown.
  • No enzymatic activity or biochemical function established
  • No structure or direct binding partner defined
  • No genetic perturbation or phenotype characterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
Regulatory motif 028 DNA-associated complex (with AP2-I, bromodomain proteins, HMGB3, SWIB/MDM2 domain protein) [#1]

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 NOP5 (PF3D7_1008800/PF10_0085) was detected in the nuclear proteome of P. falciparum by high-accuracy mass spectrometry, and is noted as one of only three proteins previously localized to the parasite nucleolus. Organellar proteomics (high-accuracy mass spectrometry of isolated nuclei) Genome biology Low 23181666
2018 NOP5 (PF3D7_1008800) was enriched in DNA pull-downs using oligonucleotide probes containing de novo regulatory motif 028, together with the transcription factor AP2-I and chromatin-related factors (bromodomain proteins, HMGB3, SWIB/MDM2 domain protein), suggesting NOP5 associates with this regulatory DNA motif complex in P. falciparum intraerythrocytic stages. DNA oligonucleotide pull-down followed by mass spectrometry Cell host & microbe Low 29649445

Source papers

Stage 0 corpus · 3 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 Assessing functional annotation transfers with inter-species conserved coexpression: application to Plasmodium falciparum. BMC genomics 13 20078859
2018 Chromatin Accessibility-Based Characterization of the Gene Regulatory Network Underlying Plasmodium falciparum Blood-Stage Development. Cell host & microbe 0 29649445
2012 Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum. Genome biology 0 23181666