FYVE zinc-finger proteins in the plant model Arabidopsis thaliana: identification of PtdIns3P-binding residues by comparison of classic and variant FYVE domains
Copyright policy )FYVE zinc-finger proteins in the plant model Arabidopsis thaliana: identification of PtdIns3P-binding residues by comparison of classic and variant FYVE domains
Classic FYVE zinc-finger domains recognize the phosphoinositide signal PtdIns3P and share the basic (R/K)1(R/K)HHCR6 (single-letter amino acid codes) consensus sequence. This domain is present in predicted PtdIns3P 5-kinases and lipases from Arabidopsis thaliana. Other Arabidopsis proteins, named PRAF, consist of a pleckstrin homology (PH) domain, a regulator of chromosome condensation (RCC1) guanine nucleotide exchange factor repeat domain, and a variant FYVE domain containing an Asn residue and a Tyr residue at positions corresponding to the PtdIns3P-interacting His4 and Arg6 of the basic motif. Dot-blot and liposome-binding assays were used in vitro to examine the phospholipid-binding ability of isolated PRAF domains. Whereas the PH domain preferentially bound PtdIns(4,5)P2, the variant FYVE domain showed a weaker charge-dependent binding of phosphoinositides. In contrast, specificity for PtdIns3P was obtained by mutagenic conversion of the variant into a classic FYVE domain (Asn4,Tyr6 → His4,Arg6). Separate substitutions of the variant residues were not sufficient to impose preferential binding of PtdIns3P, suggesting a co-operative effect of these residues in binding. A biochemical function for PRAF was indicated by its ability to catalyse guanine nucleotide exchange on some of the small GTPases of the Rab family, permitting a discussion of the biological roles of plant FYVE proteins and their regulation by phosphoinositides.
- University of Copenhagen Denmark
- University of Copenhagen Denmark
Binding Sites, Arabidopsis Proteins, GTPase-Activating Proteins, Molecular Sequence Data, Arabidopsis, Nuclear Proteins, Cell Cycle Proteins, Guanosine Diphosphate, Models, Biological, Polymerase Chain Reaction, Protein Structure, Tertiary, Phosphatidylinositol Phosphates, Gene Expression Regulation, Plant, Liposomes, Guanine Nucleotide Exchange Factors, Amino Acid Sequence, Guanosine Triphosphate, RNA, Messenger, DNA Primers, Glutathione Transferase
Binding Sites, Arabidopsis Proteins, GTPase-Activating Proteins, Molecular Sequence Data, Arabidopsis, Nuclear Proteins, Cell Cycle Proteins, Guanosine Diphosphate, Models, Biological, Polymerase Chain Reaction, Protein Structure, Tertiary, Phosphatidylinositol Phosphates, Gene Expression Regulation, Plant, Liposomes, Guanine Nucleotide Exchange Factors, Amino Acid Sequence, Guanosine Triphosphate, RNA, Messenger, DNA Primers, Glutathione Transferase
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