Literature DB >> 11866581

Toward synthetic transcription activators: recruitment of transcription factors to DNA by a PNA-peptide chimera.

Bo Liu1, Ying Han, David R Corey, Thomas Kodadek.   

Abstract

A PNA-peptide chimera designed to mimic the biochemical function of transcription activators has been synthesized and characterized. The bis-PNA segment binds specifically to a DNA site while the 20-residue peptide is capable of binding to the transcription factors Gal11 and Gal80. The PNA-peptide chimera thus mimics one of the central functions of a native transcription activator, recruitment of transcription factors to a specific DNA site.

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Year:  2002        PMID: 11866581     DOI: 10.1021/ja0164226

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  4 in total

1.  Minimization of a protein-DNA dimerizer.

Authors:  Ryan L Stafford; Hans-Dieter Arndt; Mary L Brezinski; Aseem Z Ansari; Peter B Dervan
Journal:  J Am Chem Soc       Date:  2007-02-10       Impact factor: 15.419

2.  The reach of linear protein-DNA dimerizers.

Authors:  Ryan L Stafford; Peter B Dervan
Journal:  J Am Chem Soc       Date:  2007-10-20       Impact factor: 15.419

3.  Design and synthesis of a cell-permeable synthetic transcription factor mimic.

Authors:  Xiangshu Xiao; Peng Yu; Hyun-Suk Lim; Devanjan Sikder; Thomas Kodadek
Journal:  J Comb Chem       Date:  2007-05-27

4.  End invasion of peptide nucleic acids (PNAs) with mixed-base composition into linear DNA duplexes.

Authors:  Irina V Smolina; Vadim V Demidov; Viatcheslav A Soldatenkov; Sergey G Chasovskikh; Maxim D Frank-Kamenetskii
Journal:  Nucleic Acids Res       Date:  2005-10-04       Impact factor: 16.971

  4 in total

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