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Journal of Experimental Botany, Vol. 53, No. 368, pp. 565-567, March 1, 2002
© 2002 Oxford University Press

Gene Note

PARF-1: an Arabidopsis thaliana FYVE-domain protein displaying a novel eukaryotic domain structure and phosphoinositide affinity

Begona Heras1 and Bjørn K. Drøbak2

Cell 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.

Key words: Arabidopsis thaliana, FYVE-domain, phosphoinositides, Pleckstrin Homology (PH) domain, RCC1.


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