Affinage · Plasmodium

NUF1P1

PF3D7_1473900 · ribosome assembly 1 protein

Audit flag: identity unverified
Annotated
2026-09-08
1 papers in source corpus 1 papers cited in narrative 1 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUF1P1 (PF3D7_1473900) is a Plasmodium falciparum protein implicated in ribosome assembly that has been characterized structurally through its interaction with ZNHIT3 (PMID:35315277). X-ray crystallography of the ZNHIT3–NUF1P1 complex revealed a thermally stable, species-dependent assembly in which key hydrophobic residues form the interaction interface; the ZNHIT3 fragment that engages NUF1P1 can multimerize in vitro and undergoes conformational changes that bury the hydrophobic residues required for NUF1P1 binding, regulating complex formation (PMID:35315277). Beyond this structural characterization of the ZNHIT3–NUF1P1 interface (PMID:35315277), no further in-parasite mechanistic detail — including functional validation, substrate engagement, or subcellular localization of NUF1P1 — has been characterized in the available corpus.

Mechanistic history

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

    To establish how P. falciparum NUF1P1 engages its partner ZNHIT3, this study asked what the physical basis of the interaction is and resolved the atomic structure of the complex.

    Evidence X-ray crystallography of the ZNHIT3–NUF1P1 complex with in vitro multimerization assays and AlphaFold comparison, in P. falciparum

    PMID:35315277

    Open questions at the time
    • No functional validation of NUF1P1 in the parasite; the biological consequence of the interaction is untested
    • The precise role of NUF1P1 in ribosome assembly or rRNA modification is not experimentally demonstrated here
    • Single lab, single study without independent confirmation

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether NUF1P1 functions in ribosome assembly, rRNA modification, or related pathways in the living parasite remains unestablished.
  • No in-parasite loss-of-function or localization data for NUF1P1
  • No identified substrate or downstream effector
  • No demonstration that the ZNHIT3 interaction is required for a specific cellular process

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
Complex memberships
ZNHIT3–NUF1P1 complex (PF3D7_1473900 with ZNHIT3)

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2022 NUF1P1 (NUFIP1, PF3D7_1473900) from P. falciparum forms a thermally stable, species-dependent complex with ZNHIT3; the three-dimensional structure of this complex was solved, revealing key hydrophobic residues at the interaction interface. The free ZNHIT3 fragment that binds NUF1P1 was shown to multimerize in vitro and to adopt conformational changes that bury the hydrophobic residues required for NUF1P1 binding. X-ray crystallography / structural determination of the ZNHIT3–NUFIP1 complex, in vitro biochemical characterization (multimerization assay), and comparison with AlphaFold predictions Biochemistry Medium 35315277

Source papers

Stage 0 corpus · 1 paper · ranked by NIH iCite citations
Year Title Journal Citations PMID
2022 Structural Analysis of the Plasmodial Proteins ZNHIT3 and NUFIP1 Provides Insights into the Selectivity of a Conserved Interaction. Biochemistry 5 35315277