Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor

FEBS Letters
C BergerH R Bosshard

Abstract

Basic leucine zipper (bZIP) transcription factors are dimers that recognize mainly palindromic DNA sites. It has been assumed that bZIP factors have to form a dimer in order to bind to their target DNA. We find that DNA binding of both monomeric and dimeric bZIP transcription factor GCN4 is diffusion-limited and that, therefore, the rate of dimerization of the bZIP domain does not affect the rate of DNA recognition and GCN4 need not dimerize in order to bind to its specific DNA site. The results have implications for the mechanism by which bZIP transcription factors find their target sites for transcriptional regulation.

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Citations

Feb 17, 2001·Journal of Molecular Recognition : JMR·A P Demchenko
Oct 2, 2004·Nucleic Acids Research·Anatoly I DraganPeter L Privalov
Oct 17, 2002·Protein Science : a Publication of the Protein Society·Jessica J HollenbeckMartha G Oakley
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Jul 13, 2016·The Journal of Physical Chemistry. B·Yuki AkiyamaMasahide Terazima
Jul 20, 2013·Biochemistry·Netaly KhazanovYaakov Levy
Jan 11, 2014·Journal of Chemical Theory and Computation·Paul RobustelliArthur G Palmer
Apr 16, 2015·Chemical Communications : Chem Comm·Gemma A BullenAnna F A Peacock
Jun 1, 1999·FEBS Letters·C BergerH R Bosshard
Dec 7, 2002·Journal of Theoretical Biology·R BundschuhC Jayaprakash

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