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J. Biol. Chem., Vol. 278, Issue 43, 42487-42494, October 24, 2003

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Steroidogenic Acute Regulatory Protein-binding Protein Cloned by a Yeast Two-hybrid System^*

Teruo Sugawara, Hiroshi Shimizu, Nobuhiko Hoshi¶, Ayako Nakajima||, and Seiichiro Fujimoto||

From the Department of Biochemistry, Obstetrics and Gynecology, ^||Hokkaido University Graduate School of Medicine, Sapporo 060-8638 and ^¶Laboratory of Experimental Animal Science, Kitasato University School of Veterinary Medicine and Animal Sciences, Towada 034-8628, Japan

Steroidogenic acute regulatory (StAR) protein plays a key role in the transport of cholesterol from the outer mitochondrial membrane to the inner membrane. A StAR mutant protein lacking the first 62 amino acids (N-62 StAR protein) has been reported to be as effective as wild-type StAR protein. In the present study, we examined the mechanism by which StAR protein stimulates steroidogenesis. A Gal4-based yeast two-hybrid system was used to identify proteins interacting with N-62 StAR protein. Nine positive clones were obtained from screening 1 x 10⁶ clones. The results of pull-down assays and mammalian two-hybrid assays confirmed interaction between N-62 StAR protein and the clone 4 translated product. The clone 4 translated product was named StAR-binding protein (SBP). We prepared an expression plasmid (pSBP) by inserting SBP cDNA into the pTarget vector. After cotransfection with the human cytochrome P450scc system, StAR expression vector, and pSBP, the amount of pregnenolone produced by COS-1 cells was increased. The amount of steroid hormones produced by steroidogenic cells subjected to small interfering RNA treatment was less than that produced by control cells. In conclusion, SBP binds StAR protein in cells and enhances the ability of StAR protein to promote syntheses of steroid hormones.

Received for publication, March 5, 2003 , and in revised form, August 5, 2003.

^* 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: Dept. of Biochemistry, Hokkaido University Graduate School of Medicine, Kita-ku, Kita 15, Nishi 7, Sapporo 060-8638, Japan. Tel.: 81-11-706-5047; Fax: 81-11-727-6006; E-mail: terusuga{at}med.hokudai.ac.jp.

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