Affinage · Plasmodium

RRP41

PF3D7_1427800 · exosome complex component RRP41

Annotated
2026-09-08
2 papers in source corpus 1 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1427800 (RRP41) is a catalytically active subunit of the P. falciparum RNA exosome-like complex that degrades single-stranded RNA. Recombinant PfRrp41 exhibits ribonuclease activity against ssRNA in vitro, establishing it as a catalytic component of the parasite exosome-like machinery (PMID:29664138), and the protein localizes to the cytoplasm of asexual-stage parasites (PMID:29664138). Beyond this in vitro activity and localization, no further mechanistic detail — including substrate specificity in vivo, complex partners, or functional consequences of its ribonuclease activity — has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2018 Medium

    Whether PF3D7_1427800 is itself an active nuclease or merely a structural exosome subunit was unknown; demonstrating intrinsic ribonuclease activity established it as a catalytic component of the parasite RNA exosome-like complex.

    Evidence In vitro ribonuclease activity assay with recombinant PfRrp41 against ssRNA substrate

    PMID:29664138

    Open questions at the time
    • Activity shown by a single lab with a single method and no catalytic-site mutagenesis to confirm the activity is intrinsic to RRP41
    • Substrate specificity and in vivo RNA targets not defined
    • Contribution to an assembled exosome complex not tested
  2. 2018 Medium

    The subcellular compartment in which PF3D7_1427800 operates was unknown; immunofluorescence placed the protein in the cytoplasm of asexual-stage parasites, indicating a cytoplasmic site of exosome-like RNA turnover.

    Evidence Indirect immunofluorescence assay with Western blot confirmation of expression in asexual-stage P. falciparum

    PMID:29664138

    Open questions at the time
    • Localization by indirect IFA in a single lab, not linked to a functional consequence
    • No data on nuclear versus cytoplasmic exosome distribution or stage-specific relocalization
    • Complex assembly state at the localized site not determined

Open questions

Synthesis pass · forward-looking unresolved questions
  • The identity of the in vivo RNA substrates, the composition of the RRP41-containing exosome-like complex, and the biological role of its ribonuclease activity in parasite biology remain unresolved.
  • No interacting exosome subunits or complex partners identified for PF3D7_1427800 in the corpus
  • No genetic or knockdown data linking RRP41 activity to a parasite phenotype
  • No structural model or catalytic-residue mapping

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
RNA exosome-like complex (P. falciparum)

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2018 Recombinant PfRrp41 (PF3D7_1427800) exhibited catalytic activity for single-stranded RNA (ssRNA) in vitro, establishing it as a catalytic subunit of the P. falciparum RNA exosome-like complex. In vitro ribonuclease activity assay using recombinant protein The Journal of eukaryotic microbiology Medium 29664138
2018 PfRrp41 (PF3D7_1427800) localizes to the cytoplasm of P. falciparum asexual-stage parasites, as determined by indirect immunofluorescence. Indirect immunofluorescence assay (IFA) with Western blot confirmation of protein expression The Journal of eukaryotic microbiology Medium 29664138

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2018 Characterization of the Catalytic Subunits of the RNA Exosome-like Complex in Plasmodium falciparum. The Journal of eukaryotic microbiology 5 29664138
2009 Analysis of small nucleolar RNAs reveals unique genetic features in malaria parasites. BMC genomics 0 19200392