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J. Biol. Chem., Vol. 279, Issue 51, 53544-53553, December 17, 2004

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Plants Express a Lipid Transfer Protein with High Similarity to Mammalian Sterol Carrier Protein-2^*

Johan Edqvist, Elin Rönnberg, Sara Rosenquist, Kristina Blomqvist, Lenita Viitanen¶, Tiina A. Salminen¶, Matts Nylund¶, Jessica Tuuf¶, and Peter Mattjus¶

From the Department of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences, Box 7080, 750 07 Uppsala, Sweden and the ^¶Department of Biochemistry and Pharmacy, Åbo Akademi University, P. O. Box 66, FIN-20521 Turku, Finland

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.

Received for publication, May 7, 2004 , and in revised form, September 28, 2004.

^* This work was supported by The Swedish Research Council, Carl Trygger Foundation, AgriFunGen Research Program in Functional Genomics at SLU, Academy of Finland, Sigrid Jusélius Stiftelse, Magnus Ehrnrooths Stiftelse, Svenska Kulturfonden, Medicinska Understödsföreningen Liv och Hälsa r.f., and the Åbo Akademi University. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 46-18-673242; Fax: 46-18-673279; E-mail: Johan.Edqvist{at}vbsg.slu.se.

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