Plants express a lipid transfer protein with high similarity to mammalian sterol carrier protein-2

J Edqvist, E Rönnberg, S Rosenquist, K Blomqvist, L Viitanen, Tiina Salminen, M Nylund, Jessica Tuuf, Peter Mattjus

    Tutkimustuotos: LehtiartikkeliArtikkeliTieteellinenvertaisarvioitu

    24 Sitaatiot (Scopus)

    Abstrakti

    This is the first report describing the cloning and characterization of sterol carrier protein-2 (SCP-2) from plants. Arabidopsis thaliana SCP-2 (AtSCP-2) consists of 123 amino acids with a molecular mass of 13.6 kDa. AtSCP-2 shows 35% identity and 56% similarity to the human SCP-2-like domain present in the human D-bifunctional protein (DBP) and 30% identity and 54% similarity to the human SCP-2 encoded by SCP-X. The presented structural models of apo-AtSCP-2 and the ligand-bound conformation of AtSCP-2 reveal remarkable similarity with two of the structurally known SCP-2s, the SCP-2-like domain of human DBP and the rabbit SCP-2, correspondingly. The AtSCP-2 models in both forms have a similar hydrophobic ligand-binding tunnel, which is extremely suitable for lipid binding. AtSCP-2 showed in vitro transfer activity of BODIPY-phosphatidylcholine (BODIPY-PC) from donor membranes to acceptor membranes. The transfer of BODIPY-PC was almost completely inhibited after addition of 1-palmitoyl 2-oleoyl phosphatidylcholine or ergosterol. Dimyristoyl phosphatidic acid, stigmasterol, steryl glucoside, and cholesterol showed a moderate to marginal ability to lower the BODIPY-PC transfer rate, and the single chain palmitic acid and stearoyl-coenzyme A did not affect transfer at all. Expression analysis showed that AtSCP-2 mRNA is accumulating in most plant tissues. Plasmids carrying fusion genes between green fluorescent protein and AtSCP-2 were transformed with particle bombardment to onion epidermal cells. The results from analyzing the transformants indicate that AtSCP-2 is localized to peroxisomes.
    AlkuperäiskieliEi tiedossa
    Sivut53544–53553
    Sivumäärä10
    JulkaisuJournal of Biological Chemistry
    Vuosikerta279
    Numero51
    DOI - pysyväislinkit
    TilaJulkaistu - 2004
    OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

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