Role of zinc finger structure in nuclear localization of transcription factor Sp1
Transcription factor Sp1 is localized in the nucleus and regulates gene expression. Our previous study demonstrated that the carboxyl terminal region of Sp1 containing 3-zinc finger region as DNA binding domain can also serve as nuclear localization signal (NLS). However, the nuclear transport mecha...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2009-02, Vol.380 (1), p.28-32 |
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| creator | Ito, Tatsuo Azumano, Makiko Uwatoko, Chisana Itoh, Kohji Kuwahara, Jun |
| description | Transcription factor Sp1 is localized in the nucleus and regulates gene expression. Our previous study demonstrated that the carboxyl terminal region of Sp1 containing 3-zinc finger region as DNA binding domain can also serve as nuclear localization signal (NLS). However, the nuclear transport mechanism of Sp1 has not been well understood. In this study, we performed a gene expression study on mutant Sp1 genes causing a set of amino acid substitutions in zinc finger domains to elucidate nuclear import activity. Nuclear localization of the GFP-fused mutant Sp1 proteins bearing concomitant substitutions in the first and third zinc fingers was highly inhibited. These mutant Sp1 proteins had also lost the binding ability as to the GC box sequence. The results suggest that the overall tertiary structure formed by the three zinc fingers is essential for nuclear localization of Sp1 as well as dispersed basic amino acids within the zinc fingers region. |
| doi_str_mv | 10.1016/j.bbrc.2008.12.165 |
| format | Article |
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Our previous study demonstrated that the carboxyl terminal region of Sp1 containing 3-zinc finger region as DNA binding domain can also serve as nuclear localization signal (NLS). However, the nuclear transport mechanism of Sp1 has not been well understood. In this study, we performed a gene expression study on mutant Sp1 genes causing a set of amino acid substitutions in zinc finger domains to elucidate nuclear import activity. Nuclear localization of the GFP-fused mutant Sp1 proteins bearing concomitant substitutions in the first and third zinc fingers was highly inhibited. These mutant Sp1 proteins had also lost the binding ability as to the GC box sequence. 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Our previous study demonstrated that the carboxyl terminal region of Sp1 containing 3-zinc finger region as DNA binding domain can also serve as nuclear localization signal (NLS). However, the nuclear transport mechanism of Sp1 has not been well understood. In this study, we performed a gene expression study on mutant Sp1 genes causing a set of amino acid substitutions in zinc finger domains to elucidate nuclear import activity. Nuclear localization of the GFP-fused mutant Sp1 proteins bearing concomitant substitutions in the first and third zinc fingers was highly inhibited. These mutant Sp1 proteins had also lost the binding ability as to the GC box sequence. 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Azumano, Makiko ; Uwatoko, Chisana ; Itoh, Kohji ; Kuwahara, Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-71a3f159ff8fe4c6d6af114957d070b99a44aaa8f69641b8ca3e27fadae777bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Active Transport, Cell Nucleus - drug effects</topic><topic>AMINO ACIDS</topic><topic>Aminoquinolines - pharmacology</topic><topic>Cell Nucleus - metabolism</topic><topic>DICHROISM</topic><topic>DNA</topic><topic>ELECTROPHORESIS</topic><topic>GC box</topic><topic>GENES</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>MUTANTS</topic><topic>Nuclear localization signal</topic><topic>Nuclear Localization Signals - genetics</topic><topic>Nuclear Localization Signals - physiology</topic><topic>Sp1</topic><topic>Sp1 Transcription Factor - genetics</topic><topic>Sp1 Transcription Factor - metabolism</topic><topic>SULFONAMIDES</topic><topic>Tosyl Compounds - pharmacology</topic><topic>TRANSCRIPTION FACTORS</topic><topic>ZINC</topic><topic>Zinc - metabolism</topic><topic>Zinc finger</topic><topic>Zinc Fingers - genetics</topic><topic>Zinc Fingers - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ito, Tatsuo</creatorcontrib><creatorcontrib>Azumano, Makiko</creatorcontrib><creatorcontrib>Uwatoko, Chisana</creatorcontrib><creatorcontrib>Itoh, Kohji</creatorcontrib><creatorcontrib>Kuwahara, Jun</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ito, Tatsuo</au><au>Azumano, Makiko</au><au>Uwatoko, Chisana</au><au>Itoh, Kohji</au><au>Kuwahara, Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of zinc finger structure in nuclear localization of transcription factor Sp1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2009-02-27</date><risdate>2009</risdate><volume>380</volume><issue>1</issue><spage>28</spage><epage>32</epage><pages>28-32</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Transcription factor Sp1 is localized in the nucleus and regulates gene expression. Our previous study demonstrated that the carboxyl terminal region of Sp1 containing 3-zinc finger region as DNA binding domain can also serve as nuclear localization signal (NLS). However, the nuclear transport mechanism of Sp1 has not been well understood. In this study, we performed a gene expression study on mutant Sp1 genes causing a set of amino acid substitutions in zinc finger domains to elucidate nuclear import activity. Nuclear localization of the GFP-fused mutant Sp1 proteins bearing concomitant substitutions in the first and third zinc fingers was highly inhibited. These mutant Sp1 proteins had also lost the binding ability as to the GC box sequence. The results suggest that the overall tertiary structure formed by the three zinc fingers is essential for nuclear localization of Sp1 as well as dispersed basic amino acids within the zinc fingers region.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19138671</pmid><doi>10.1016/j.bbrc.2008.12.165</doi><tpages>5</tpages></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES Active Transport, Cell Nucleus - drug effects AMINO ACIDS Aminoquinolines - pharmacology Cell Nucleus - metabolism DICHROISM DNA ELECTROPHORESIS GC box GENES HeLa Cells Humans MUTANTS Nuclear localization signal Nuclear Localization Signals - genetics Nuclear Localization Signals - physiology Sp1 Sp1 Transcription Factor - genetics Sp1 Transcription Factor - metabolism SULFONAMIDES Tosyl Compounds - pharmacology TRANSCRIPTION FACTORS ZINC Zinc - metabolism Zinc finger Zinc Fingers - genetics Zinc Fingers - physiology |
| title | Role of zinc finger structure in nuclear localization of transcription factor Sp1 |
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