Affinage · Plasmodium

SNU13

PF3D7_1123900 · 13 kDa ribonucleoprotein-associated protein, putative

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1123900 (SNU13) is a nuclear protein of Plasmodium falciparum identified in the experimentally determined core nuclear proteome by high-accuracy mass spectrometry, where network analysis positioned it as a central node bridging clusters assigned to mRNA splicing/processing, the nucleolus, and translation initiation (PMID:23181666). Beyond this localization and network placement, no direct biochemical or functional experiment has been performed on the P. falciparum protein itself; its assignment as a box C/D snoRNP component (with fibrillarin, Nop56, and Nop58) rests on computational homology rather than experiment (PMID:19200392), and its detection as a proximity interactor of PfSAMS and PfSET10 comes from single proximity-labeling screens with bioinformatic network interpretation (PMID:35889137, PMID:39445823). The corpus therefore establishes SNU13 as a nuclear, network-central protein linked by inference to spliceosomal, ribosome-biogenesis, and translation-associated machinery, but no molecular activity of PF3D7_1123900 has been directly demonstrated.

Mechanistic history

Synthesis pass · year-by-year structured walk · 4 steps
  1. 2009 Low

    To ask whether malaria parasites possess the conserved rRNA-modification machinery, a homology search tested whether a SNU13 homologue exists as part of the box C/D snoRNP.

    Evidence Computational PSI-BLAST homology search across Plasmodium genomes

    PMID:19200392

    Open questions at the time
    • Purely computational prediction with no biochemical validation on the Plasmodium protein
    • snoRNP membership and rRNA 2'-O-methylation role not experimentally confirmed for PF3D7_1123900
    • No demonstration of physical association with fibrillarin, Nop56, or Nop58 in the parasite
  2. 2012 Medium

    To establish where PF3D7_1123900 acts, nuclear proteomics placed it experimentally in the core nuclear proteome and network analysis identified it as a hub connecting splicing/processing, nucleolar, and translation-initiation clusters.

    Evidence High-accuracy mass spectrometry of nuclear fractions with STRING network analysis in P. falciparum

    PMID:23181666

    Open questions at the time
    • Network centrality is bioinformatic inference, not a functional assay
    • No direct molecular activity assigned to the protein
    • Does not distinguish which of the linked processes SNU13 directly participates in
  3. 2022 Low

    A proximity-labeling screen around PfSAMS tested SNU13's local environment and placed it as an intermediary linking the spliceosome cluster to translation initiation factors.

    Evidence BioID/TurboID proximity labeling coupled to mass spectrometry with STRING network analysis in blood-stage parasites

    PMID:35889137

    Open questions at the time
    • Single proximity-labeling experiment; proximity does not establish a direct or functional interaction
    • Network role is bioinformatic inference
    • No reciprocal validation of the PfSAMS association
  4. 2024 Low

    A TurboID screen around PfSET10 again recovered SNU13, reinforcing its network position bridging mRNA processing, ribosomes/translation, and spliceosome clusters.

    Evidence TurboID proximity labeling coupled to mass spectrometry with STRING network analysis in blood-stage parasites

    PMID:39445823

    Open questions at the time
    • Single proximity-labeling experiment in one lab
    • Network centrality is bioinformatic, not functional
    • Does not establish a direct SNU13–PfSET10 interaction or a shared pathway

Open questions

Synthesis pass · forward-looking unresolved questions
  • No direct biochemical or functional experiment has defined the molecular activity, RNA/protein partners, or in vivo role of PF3D7_1123900 itself; whether it functions in box C/D snoRNP-mediated rRNA methylation, spliceosome assembly, or translation remains experimentally unresolved.
  • No knockout, knockdown, or complementation phenotype for PF3D7_1123900
  • No demonstrated RNA-binding or snoRNP assembly activity in the parasite
  • No structural or reconstitution data on the P. falciparum protein

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
box C/D snoRNP (predicted by homology only) [#3]

Evidence

Reading pass · 4 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 SNU13 (PF3D7_1123900) was detected as a nuclear protein in P. falciparum by high-accuracy mass spectrometry-based nuclear proteomics, placing it in the experimentally determined core nuclear proteome. Network analysis of the nuclear proteome identified SNU13 as a central node connecting clusters assigned to mRNA splicing/processing, the nucleolus, and translation initiation. High-accuracy mass spectrometry of nuclear fractions; STRING-based protein-protein interaction network analysis Genome biology Medium 23181666
2022 SNU13 (PF3D7_1123900) was identified as an interactor of PfSAMS (S-adenosylmethionine synthetase) in a proximity-dependent biotin identification (TurboID/BioID) screen, and network analysis placed it as the intermediary connecting the spliceosome protein cluster to the translation initiation factor cluster in P. falciparum blood-stage parasites. Proximity-dependent biotin identification (BioID/TurboID) coupled to mass spectrometry; STRING interaction network analysis Microorganisms Low 35889137
2024 SNU13 (PF3D7_1123900) was identified as an interactor of PfSET10 by TurboID coupled with mass spectrometry in P. falciparum blood-stage parasites; network analysis placed SNU13 as a central protein connecting clusters related to mRNA processing, ribosomes/translation, and spliceosome function within the PfSET10 interaction network. TurboID proximity labeling coupled to mass spectrometry; STRING-based protein-protein interaction network analysis mSphere Low 39445823
2009 A P. falciparum homologue of SNU13 was identified bioinformatically as a component of the box C/D snoRNP complex (alongside fibrillarin, Nop56, and Nop58), implicating it in rRNA 2'-O-ribose methylation and ribosome biogenesis in malaria parasites. Computational homology search (PSI-BLAST) across Plasmodium genomes BMC genomics Low 19200392

Source papers

Stage 0 corpus · 10 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum. Genome biology 120 23181666
2024 The Plasmodium falciparum histone methyltransferase SET10 participates in a chromatin modulation network crucial for intraerythrocytic development. mSphere 0 39445823
2023 Integrating Phylogenetics With Intron Positions Illuminates the Origin of the Complex Spliceosome. Molecular biology and evolution 0 36631250
2023 Spliceosome assembly and regulation: insights from analysis of highly reduced spliceosomes. RNA (New York, N.Y.) 0 36737103
2022 Probing small ribosomal subunit RNA helix 45 acetylation across eukaryotic evolution. Nucleic acids research 0 35648437
2022 Plasmodium falciparum S-Adenosylmethionine Synthetase Is Essential for Parasite Survival through a Complex Interaction Network with Cytoplasmic and Nuclear Proteins. Microorganisms 0 35889137
2020 Naturally occurring modified ribonucleosides. Wiley interdisciplinary reviews. RNA 0 32301288
2015 Contrasting host-pathogen interactions and genome evolution in two generalist and specialist microsporidian pathogens of mosquitoes. Nature communications 0 25968466
2013 Origin and evolution of the eukaryotic SSU processome revealed by a comprehensive genomic analysis and implications for the origin of the nucleolus. Genome biology and evolution 0 24214024
2009 Analysis of small nucleolar RNAs reveals unique genetic features in malaria parasites. BMC genomics 0 19200392