Research
Print page Print page
Switch language
Rigshospitalet - a part of Copenhagen University Hospital
Published

FYVE zinc-finger proteins in the plant model Arabidopsis thaliana: identification of PtdIns3P-binding residues by comparison of classic and variant FYVE domains

Research output: Contribution to journalJournal articleResearchpeer-review

  1. Two transgenic mouse models for β-subunit components of succinate-CoA ligase yielding pleiotropic metabolic alterations

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Crystal structures of the ligand binding region of uPARAP: effect of calcium ion binding

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Human insulin-like growth factor II leader 2 mediates internal initiation of translation

    Research output: Contribution to journalJournal articleResearchpeer-review

  1. Evaluation of Serum Insulin-like Factor 3 Quantification by LC-MS/MS as a Biomarker of Leydig Cell Function

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Increases in bioactive IGF do not parallel increases in total IGF-I during growth hormone treatment of children born SGA

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Sex-specific estrogen levels and reference intervals from infancy to late adulthood determined by LC-MS/MS

    Research output: Contribution to journalJournal articleResearchpeer-review

  4. CENTRAL PRECOCIOUS PUBERTY IN TWO BOYS WITH PRADER-WILLI SYNDROME ON GROWTH HORMONE TREATMENT

    Research output: Contribution to journalJournal articleResearchpeer-review

  5. Fatty Liver Among Adolescent Offspring of Women With Type 1 Diabetes (the EPICOM Study)

    Research output: Contribution to journalJournal articleResearchpeer-review

View graph of relations

Classic FYVE zinc-finger domains recognize the phosphoinositide signal PtdIns3P and share the basic (R/K)(1)(R/K)HHCR(6) (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 His(4) and Arg(6) 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)P(2), 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 (Asn(4),Tyr(6)-->His(4),Arg(6)). 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.

Original languageEnglish
JournalBiochemical Journal
Volume359
Issue numberPt 1
Pages (from-to)165-73
Number of pages9
ISSN0264-6021
Publication statusPublished - 1 Oct 2001

    Research areas

  • Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Binding Sites, Cell Cycle Proteins, DNA Primers, GTPase-Activating Proteins, Gene Expression Regulation, Plant, Glutathione Transferase, Guanine Nucleotide Exchange Factors, Guanosine Diphosphate, Guanosine Triphosphate, Liposomes, Models, Biological, Molecular Sequence Data, Nuclear Proteins, Phosphatidylinositol Phosphates, Polymerase Chain Reaction, Protein Structure, Tertiary, RNA, Messenger, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Zinc Fingers, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't

ID: 49497200