Affinage · Plasmodium

RFC5

PF3D7_1111100 · replication factor C subunit 5, putative

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RFC5 (PF3D7_1111100) is a putative subunit of the replication factor C clamp-loader complex in Plasmodium falciparum that has been characterized in the available corpus only through its connection to the malarial CDK Pfmrk (PMID:20332005). It was identified as a physical interactor of Pfmrk in a bacterial two-hybrid screen and is a substrate of Pfmrk-mediated phosphorylation, with the Pfmrk activator PfMAT1 conferring substrate specificity to the kinase complex for this reaction (PMID:20332005). This links RFC5 to potential cell-cycle-dependent regulation of the parasite's DNA replication machinery. Beyond this interaction and phosphorylation relationship (PMID:20332005), no further mechanistic detail — including any direct demonstration of clamp-loader activity, DNA-binding, or subunit assembly for RFC5 itself — has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2010 Medium

    To connect the malarial CDK Pfmrk to a cellular process, an unbiased interactor search was needed; identifying RFC5 as a binding partner and phosphorylation substrate established a candidate link between Pfmrk signaling and the parasite DNA replication apparatus.

    Evidence Bacterial two-hybrid screen of a P. falciparum cDNA library, in vitro kinase assay, and co-immunoprecipitation validation of the Pfmrk–PfMAT1 complex

    PMID:20332005

    Open questions at the time
    • Direct RFC5–Pfmrk interaction was not confirmed by reciprocal Co-IP
    • Phosphorylation was shown in vitro in a single study; in vivo phosphosite and functional consequence for RFC5 are undefined
    • No demonstration that RFC5 functions as a clamp-loader subunit or participates in DNA replication in the parasite

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether Pfmrk-mediated phosphorylation of RFC5 regulates its assembly into the replication factor C complex or its clamp-loading function during parasite DNA replication remains unresolved.
  • No functional assay of RFC5 clamp-loader activity
  • No structural or complex-assembly data for RFC5 in P. falciparum
  • Phenotypic consequence of RFC5 phosphorylation for parasite replication is unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
PFMAT1 (PFMRK ACTIVATOR, CONFERS SUBSTRATE SPECIFICITY)PFMRK (MALARIAL CDK)
Complex memberships
replication factor C complex (putative subunit)

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 RFC5 (PfRFC-5) was identified as a physical interactor of the malarial CDK Pfmrk via bacterial two-hybrid screen of a P. falciparum cDNA library, and was demonstrated to be a substrate of Pfmrk-mediated phosphorylation; PfMAT1 (the Pfmrk activator) confers substrate specificity to the Pfmrk kinase complex for this phosphorylation. Bacterial two-hybrid screen (interaction identification); in vitro kinase assay (phosphorylation of PfRFC-5 by Pfmrk); co-immunoprecipitation (Pfmrk–PfMAT1 complex validation) Molecular and biochemical parasitology Medium 20332005

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 The malarial CDK Pfmrk and its effector PfMAT1 phosphorylate DNA replication proteins and co-localize in the nucleus. Molecular and biochemical parasitology 26 20332005
2005 Evolutionary clues to eukaryotic DNA clamp-loading mechanisms: analysis of the functional constraints imposed on replication factor C AAA+ ATPases. Nucleic acids research 0 16082778