Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
UniProt entry Q26789 (73 kDa paraflagellar rod protein)
The major components of the paraflagellar rod of Trypanosoma brucei are two similar, but distinct proteins which are encoded by two different gene loci.
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Cloning of the 73 kDa PFR protein genes; PFR-C is related to but distinct from the 69 kDa PFR-A, suggesting heteropolymeric PFR fibres.
"The present study reports the characterization of the genes coding for the 73-kDa PFR protein from T. brucei."
Paraflagellar rod is vital for trypanosome motility.
Protein transport and flagellum assembly dynamics revealed by analysis of the paralysed trypanosome mutant snl-1.
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In the absence of PFRA, PFRC enters the flagellum but accumulates unassembled at the distal tip.
"other PFR proteins such as the second major constituent, PFRC, accumulated at the distal tip of the growing flagellum, forming a large dilation or 'blob'."
Flagellar morphogenesis: protein targeting and assembly in the paraflagellar rod of trypanosomes.
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PFRA and PFRC are abundant flagellum-restricted proteins sharing a conserved distal-tip addition motif.
"This seven-amino-acid sequence is conserved in all PFRA and PFRC proteins and shows homology to a sequence in the flagellar dynein heavy chain of Chlamydomonas reinhardtii."
Flagellum ontogeny in trypanosomes studied via an inherited and regulated RNA interference system.
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PFR is composed of PFRA and PFRC and assembled at the distal tip into a stable cytoskeletal structure.
"The PFR is composed of 2 major proteins, PFRA and PFRC."
Calmodulin-binding properties of the paraflagellar rod complex from Trypanosoma brucei.
Efficiency and specificity of RNA interference generated by intra- and intermolecular double stranded RNA in Trypanosoma brucei.
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PFRC dsRNA was used in RNAi experiments; the abstract reports PFRA results only.
"PFRA and PFRC genes, which code for flagellar proteins required for cell motility."
The paraflagellar rod of kinetoplastid parasites: from structure to components and function.
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Calmodulin-Sepharose binding was assayed on a bulk purified PFR protein pool, without resolving PFR1 from PFR2, and the authors note that co-purifying PAR1/PAR4 homologues of similar molecular weight may explain the result.
"This suggests that there are two pools of PFR proteins that are differentiated by their ability to bind calmodulin, although the presence in the preparations of proteins of similar molecular weight such as PAR1 and PAR4 homologues may also explain these results."
A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
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PFR1 and PFR2 are the only PFR-localised proteins whose ablation abolishes PFR assembly; no binary interactions with other PFR proteins were detected for them.
"It is perhaps surprising that, given the central role of PFR1 and PFR2 in the PFR, no interactions were detected between these two proteins and any of the others in this study."
Calmodulin is required for paraflagellar rod assembly and flagellum-cell body attachment in trypanosomes.
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Calmodulin resides in the PFR and is required for PFR assembly.
"CaM depletion resulted in total and catastrophic failure in PFR assembly; even connections linking axoneme to PFR failed to form following CaM depletion."
Control of assembly of extra-axonemal structures: the paraflagellar rod of trypanosomes.
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PFR1 and PFR2 are the most abundant PFR proteins, critical for assembly, and are incorporated at the distal tip; they are destabilised without the cytoplasmic assembly factor PFR-AF1.
"In the PFR-AF1 null mutant, PFR1 and PFR2 protein amount increased when the cells were treated with the proteasome inhibitor MG132 suggesting that, without PFR-AF1, PFR1 and PFR2 were unstable and degraded."
Structure of the trypanosome paraflagellar rod and insights into non-planar motility of eukaryotic cells.
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Cryo-ET structure of the T. brucei PFR; PFR1 and PFR2 are essential, non-redundant structural components whose long helices may contribute to coiled-coil wires.
"suggesting that multiple subunits of PFR1 and PFR2 molecules could contribute to each arm of the wire."