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

Abstract

Research highlights: {yields} Sp1 zinc fingers themselves interact with importin {alpha}. {yields} Sp1 zinc finger domains play an essential role as a nuclear localization signal. {yields} Sp1 can be transported into the nucleus in an importin-dependent manner. -- Abstract: 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 {alpha} 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 Sp1 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.

Authors:
 [1]; ; ;  [2];  [1];  [2]
  1. Department of Medicinal Biotechnology, Institute for Medicinal Research, Graduate School of Pharmaceutical Sciences, The University of Tokushima, 1-78 Sho-machi, Tokushima 770-8505 (Japan)
  2. Department of Molecular Biophysical Chemistry, Faculty of Pharmaceutical Sciences, Doshisha Women's University, Kodo, Kyotanabe City, Kyoto 610-0395 (Japan)
Publication Date:
OSTI Identifier:
22204706
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 403; Journal Issue: 2; Other Information: Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; DNA; FLUORESCENCE; GLUTATHIONE; HELA CELLS; MALTOSE; MBP; TRANSCRIPTION FACTORS

Citation Formats

Ito, Tatsuo, Kitamura, Haruka, Uwatoko, Chisana, Azumano, Makiko, Itoh, Kohji, E-mail: kitoh@ph.tokushima-u.ac.jp, and Kuwahara, Jun, E-mail: jkuwahar@dwc.doshisha.ac.jp. Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1. United States: N. p., 2010. Web. doi:10.1016/J.BBRC.2010.10.036.
Ito, Tatsuo, Kitamura, Haruka, Uwatoko, Chisana, Azumano, Makiko, Itoh, Kohji, E-mail: kitoh@ph.tokushima-u.ac.jp, & Kuwahara, Jun, E-mail: jkuwahar@dwc.doshisha.ac.jp. Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1. United States. doi:10.1016/J.BBRC.2010.10.036.
Ito, Tatsuo, Kitamura, Haruka, Uwatoko, Chisana, Azumano, Makiko, Itoh, Kohji, E-mail: kitoh@ph.tokushima-u.ac.jp, and Kuwahara, Jun, E-mail: jkuwahar@dwc.doshisha.ac.jp. Fri . "Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1". United States. doi:10.1016/J.BBRC.2010.10.036.
@article{osti_22204706,
title = {Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1},
author = {Ito, Tatsuo and Kitamura, Haruka and Uwatoko, Chisana and Azumano, Makiko and Itoh, Kohji, E-mail: kitoh@ph.tokushima-u.ac.jp and Kuwahara, Jun, E-mail: jkuwahar@dwc.doshisha.ac.jp},
abstractNote = {Research highlights: {yields} Sp1 zinc fingers themselves interact with importin {alpha}. {yields} Sp1 zinc finger domains play an essential role as a nuclear localization signal. {yields} Sp1 can be transported into the nucleus in an importin-dependent manner. -- Abstract: 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 {alpha} 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 Sp1 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.},
doi = {10.1016/J.BBRC.2010.10.036},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 403,
place = {United States},
year = {2010},
month = {12}
}