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Diffusion‐controlled DNA recognition by an unfolded, monomeric bZIP transcription factor
Author(s) -
Berger Christine,
Piubelli Luciano,
Haditsch Ursula,
Rudolf Bosshard Hans
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00156-2
Subject(s) - bzip domain , leucine zipper , transcription factor , basic helix loop helix leucine zipper transcription factors , dna , dimer , eukaryotic transcription , zipper , atf3 , palindromic sequence , transcription (linguistics) , chemistry , dna binding domain , biology , dna binding protein , microbiology and biotechnology , biochemistry , promoter , palindrome , gene , gene expression , genome , linguistics , philosophy , organic chemistry , algorithm , computer science
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.