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Updated: Oct 2, 2026

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
Published on: July 27, 2017
PARF-1: an Arabidopsis thaliana FYVE-domain protein displaying a novel eukaryotic domain structure and
1Cell Signalling Group, Department of Disease and Stress Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.
Abstract:
A full-length cDNA encoding a novel protein named PARF-1 was isolated from Arabidopsis thaliana. PARF-1 is the first eukaryotic protein to be identified that displays a domain structure which includes a FYVE-finger domain, a Pleckstrin Homology (PH) domain, as well as multiple Regulator of Chromosome Condensation-1 (RCC1) repeats. Northern blot analysis revealed that PARF-1 mRNA is present at high levels in flowers, but only at very low levels in other tissues. Recombinant PARF-1 fusion proteins expressed in E. coli were found to display unique binding specificities for monophosphorylated phosphoinositide lipids. The unusual domain structure of PARF-1 combined with its phosphoinositide specificity suggests that it may fulfil unexpected functions in higher plants.
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