CAF1C

PF3D7_0110700 (CAF1C) is a Plasmodium falciparum histone chaperone that directly binds histone H4, established by a pulldown assay with purified recombinant protein and consistent with a role as the RbAp46/48-like subunit of the chromatin assembly factor-1 complex (PMID:32363442). The protein localizes to the nucleus and is expressed across all three asexual blood stages (ring, trophozoite, schizont) (PMID:32363442). Beyond this direct H4-binding activity and nuclear localization, the molecular mechanism and in vivo function of PF3D7_0110700 have not been characterized in the available corpus; its assignment to the CAF-1 complex and its seven-bladed WD40 β-propeller architecture rest on in silico comparison to RbAp46/48 homologs rather than on experimental structural or functional validation (PMID:32363442).

1. 2020 Medium

   To test whether PF3D7_0110700 acts as a histone chaperone, its physical association with core histones was probed, establishing a direct H4-binding activity that anchors its candidate chromatin-assembly role.

   Evidence In vitro pulldown assay with purified recombinant PF3D7_0110700 and histone H4 (protein from E. coli)

   PMID:32363442

   Open questions at the time

   • Single pulldown method without orthogonal validation or binding-interface mutagenesis
   • Binding to other histones and to assembled nucleosomes not tested
   • Whether the interaction occurs in vivo or within an intact CAF-1 complex is unresolved
2. 2020 Low

   To place the H4-binding activity in a cellular context, subcellular localization and stage expression were assessed, showing nuclear residence throughout asexual blood-stage development consistent with a chromatin function.

   Evidence Subcellular localization/fractionation assay and stage expression detection (western blot or equivalent) across ring, trophozoite, and schizont stages

   PMID:32363442

   Open questions at the time

   • Localization reported without demonstrated functional consequence and without orthogonal methods
   • No evidence linking nuclear presence to chromatin assembly activity in vivo
   • Gametocyte and other life-cycle stages not examined
3. 2020 Low

   To classify PF3D7_0110700 structurally, comparative modeling was used, inferring a conserved seven-bladed WD40 β-propeller and RbAp46/48-like binding interfaces with species-specific features distinguishing it from yeast, Drosophila, and human orthologs.

   Evidence Comparative in silico sequence and structural analysis

   PMID:32363442

   Open questions at the time

   • Computational inference only, with no experimental structure
   • CAF-1 complex membership predicted by homology, not demonstrated biochemically
   • Functional significance of the species-specific features untested

• The in vivo function of PF3D7_0110700, its assembly into and role within a Plasmodium CAF-1 complex, and its contribution to parasite chromatin assembly and viability remain unresolved.
• No knockout, knockdown, or conditional-depletion phenotype reported
• CAF-1 complex partners not experimentally identified for this subunit
• No experimental structure or nucleosome-assembly assay