PARF-1: an Arabidopsis thaliana FYVE-domain protein displaying a novel eukaryotic domain structure and phosphoinositide affinity.
J Exp Bot
; 53(368): 565-7, 2002 Mar.
Article
in En
| MEDLINE
| ID: mdl-11847256
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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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phosphatidylinositols
/
Arabidopsis
/
Arabidopsis Proteins
Language:
En
Journal:
J Exp Bot
Journal subject:
BOTANICA
Year:
2002
Type:
Article
Affiliation country:
United kingdom