Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1

被引：21

作者：

Ito, Tatsuo ^{[1
]}

Kitamura, Haruka ^{[2
]}

Uwatoko, Chisana ^{[2
]}

Azumano, Makiko ^{[2
]}

Itoh, Kohji ^{[1
]}

Kuwahara, Jun ^{[2
]}

机构：

[1] Univ Tokushima, Dept Med Biotechnol, Inst Med Res, Grad Sch Pharmaceut Sci, Tokushima 7708505, Japan

[2] Doshisha Womens Univ, Dept Mol Biophys Chem, Fac Pharmaceut Sci, Kyotanabe, Kyoto 6100395, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 403卷 / 02期

关键词：

Sp1; Zinc finger; Nuclear localization signal; Importin alpha; Importin beta; MAMMALIAN IMPORTIN-ALPHA; NUCLEOCYTOPLASMIC TRANSPORT; HUMAN HOMOLOG; DNA-BINDING; PROTEIN; SIGNAL; DOMAIN; IDENTIFICATION; SEQUENCE; RECEPTOR;

D O I：

10.1016/j.bbrc.2010.10.036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transcription factor Sp1 is localized in the nucleus and regulates the expression of many cellular genes, but the nuclear transport mechanism of Sp1 is not well understood. In this study, we revealed that GST-fused Sp1 protein bound to endogenous importin a in HeLa cells via the Sp1 zinc finger domains, which comprise the DNA binding domain of Sp1. It was found that the Sp1 zinc finger domains directly interacted with a wide range of importin alpha including the armadillo (arm) repeat domain and the C-terminal acidic domain. Furthermore, it turned out that all three zinc fingers of So are essential for binding to importin alpha. Taken together, these results suggest that the Sp1 zinc finger domains play an essential role as a NLS and Sp1 can be transported into the nucleus in an importin-dependent manner even though it possesses no classical NLSs. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：161 / 166

页数：6

共 29 条

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