PARF-1: an Arabidopsis thaliana FYVE-domain protein displaying a novel eukaryotic domain structure and phosphoinositide affinity.
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.
Heras
Begoña
B
Cell Signalling Group, Department of Disease and Stress Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.
Drøbak
Bjørn K
BK
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics*; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites / Q000235:genetics; D001667:Binding, Competitive; D015152:Blotting, Northern; D018506:Gene Expression Regulation, Plant; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000378:metabolism*; D018514:Plant Structures / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D016335:Zinc Fingers / Q000235:genetics
D029681:Arabidopsis Proteins; C454959:PARF-1 protein, Arabidopsis; D010716:Phosphatidylinositols; D012333:RNA, Messenger