Affinage · Plasmodium

TAF10

PF3D7_0522200 · transcription initiation factor TFIID subunit 10, putative

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0522200 (TAF10) is a predicted TFIID-associated subunit of Plasmodium falciparum that participates in an atypical transcription initiation module rather than a classical TFIID complex (PMID:16042788, PMID:31728527). It was originally identified computationally as a putative ortholog of TFIID subunit TAF10, in an analysis that found no P. falciparum TAFs bearing classical histone-fold domains, indicating an unusual architecture for the parasite TFIID (PMID:16042788). Interaction proteomics subsequently placed TAF10 within a co-purifying TAF complex that includes BDP5/TAF1, TAF2, and a WD-repeat hTAF5 homolog (PF3D7_1138800) together with five apicomplexan-specific proteins; notably, this complex does not detectably associate with either P. falciparum TBP homolog, arguing that TAF10 acts in an alternative, non-canonical initiation module (PMID:31728527). Beyond its membership in this complex, no direct molecular activity, structural detail, or transcriptional function has been characterized for TAF10 itself in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2005 Low

    Establishing whether P. falciparum encodes recognizable TFIID subunits addressed whether the parasite possesses conventional basal transcription machinery; the analysis identified TAF10 as a candidate while revealing that classical histone-fold TAFs are absent.

    Evidence Computational sequence analysis (HCA and PSI-BLAST profile methods) in P. falciparum

    PMID:16042788

    Open questions at the time
    • Prediction only — no experimental validation that PF3D7_0522200 functions as a TAF10 ortholog
    • Does not establish complex membership, localization, or transcriptional activity
    • Unusual TFIID architecture inferred from absence of histone-fold TAFs, not directly demonstrated
  2. 2019 Medium

    Whether the predicted TAF10 physically assembles into a TFIID-like complex was unknown; interaction proteomics showed it co-purifies with BDP5/TAF1, TAF2, an hTAF5 homolog, and apicomplexan-specific proteins but not with either TBP homolog, establishing TAF10 as part of a non-canonical initiation module rather than a classical TFIID.

    Evidence Immunoprecipitation followed by quantitative mass spectrometry (IP-MS/MS) in P. falciparum

    PMID:31728527

    Open questions at the time
    • Single Co-IP/MS experiment from one lab without reciprocal pull-down anchored on TAF10 itself
    • Direct role of TAF10 within the complex (structural, stabilizing, or regulatory) not defined
    • Functional consequence of the absent TBP interaction for transcription initiation not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • The intrinsic molecular activity of TAF10, its requirement for parasite viability, and the genes or promoters regulated by its non-canonical TAF complex remain undefined.
  • No loss-of-function or essentiality data for TAF10 specifically
  • No structural model of the parasite TAF complex or of TAF10 within it
  • No identification of target promoters or transcriptional output of the module

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
Non-canonical P. falciparum TAF complex (BDP5/TAF1, TAF2, hTAF5 homolog PF3D7_1138800, five apicomplexan-specific proteins; no TBP association) [#1]

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 PF3D7_0522200 (TAF10) was predicted as a putative ortholog of TFIID subunit TAF10 in P. falciparum using hydrophobic cluster analysis (HCA) and PSI-BLAST profile-based methods. Notably, no candidates for TAFs with classical histone fold domains (HFDs) were found in P. falciparum, suggesting an unusual architecture of the TFIID complex in the parasite. Computational sequence analysis (HCA and PSI-BLAST) BMC genomics Low 16042788
2019 PF3D7_0522200 (TAF10) was identified as a co-purifying interactor of BDP5/TAF1 by interaction proteomics (IP-MS/MS), placing TAF10 within a putative TAF complex in P. falciparum. This complex also contains TAF2 and a WD-repeat protein homologous to hTAF5 (PF3D7_1138800), along with five apicomplexan-specific proteins. Importantly, no interaction of this TAF complex with either TBP homologue was detected, suggesting this is not a canonical TFIID complex but an alternative transcription initiation module. Immunoprecipitation followed by quantitative mass spectrometry (IP-MS/MS) Nucleic acids research Medium 31728527

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 Prediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: conserved features and differences relative to other eukaryotes. BMC genomics 101 16042788
2026 Global-scale population genetic analysis of Plasmodium falciparum identifies region-specific patterns of malaria parasite adaptation. Nature communications 0 42115185
2019 Epigenetic reader complexes of the human malaria parasite, Plasmodium falciparum. Nucleic acids research 0 31728527
2010 Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution. Biology direct 0 20132544
2008 Regulatory hotspots in the malaria parasite genome dictate transcriptional variation. PLoS biology 0 18828674