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We have conducted a protein interaction study of components within a specific sub-compartment of a eukaryotic flagellum. The trypanosome flagellum contains a para-crystalline extra-axonemal structure termed the paraflagellar rod (PFR) with around forty identified components. We have used a Gateway cloning approach coupled with yeast two-hybrid, RNAi and 2D DiGE to define a protein-protein interaction network taking place in this structure. We define two clusters of interactions; the first being characterised by two proteins with a shared domain which is not sufficient for maintaining the interaction. The other cohort is populated by eight proteins, a number of which possess a PFR domain and sub-populations of this network exhibit dependency relationships. Finally, we provide clues as to the structural organisation of the PFR at the molecular level. This multi-strand approach shows that protein interactome data can be generated for insoluble protein complexes.

Original publication




Journal article


PLoS One

Publication Date





Animals, Cloning, Molecular, Epitopes, Flagella, Genetic Techniques, Genetic Vectors, Genomics, Microscopy, Electron, Models, Biological, Open Reading Frames, Protein Interaction Mapping, Proteomics, RNA Interference, Trypanosoma brucei brucei, Two-Hybrid System Techniques