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Hideki Yamasaki^1,2,, Toshihiro Sekimoto^3,, Tadashi Ohkubo¹, Tsutomu Douchi², Yukihiro Nagata², Masayuki Ozawa¹ and Yoshihiro Yoneda^3,*

¹ Department of Biochemistry and Molecular Biology, and ² Department of Gynecology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8520, Japan
³ Department of Frontier Biosciences, Graduate School of Frontier Biosciences, Osaka University, Osaka 565-0871, Japan

Snail, a DNA-binding zinc finger protein, functions as a transcriptional repressor for genes including E-cadherin during development and the acquisition of tumor cell invasiveness. Human Snail is a 264-amino acid nuclear protein with an amino-terminal basic amino acid-rich domain (SNAG domain) and a carboxyl-terminal DNA-binding domain (zinc finger domain). A series of fusion proteins composed of green fluorescent protein (GFP) and portions of the Snail protein were generated, and their subcellular localization was examined. Fusion of the four zinc fingers to GFP led to the targeting of GFP to the nucleus, demonstrating that the zinc finger domain is sufficient for nuclear localization. Using an in vitro transport system, the nuclear import of Snail was reconstituted by importin (karyopherin) ß in the presence of Ran and NTF2. We further demonstrated that Snail binds directly to importin ß in a zinc finger domain-dependent manner. These results indicate that zinc finger domain of Snail functions as a nuclear localization signal and Snail can be transported into the nucleus in an importin ß-mediated manner.

These authors contributed equally to the article.

^* Correspondence: E-mail: yyoneda{at}anat3.med.osaka-u.ac.jp. mozawa{at}m.kufm.kagoshima-u.ac.jp

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