Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor.
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.
Berger
C
C
Biochemisches Institut der Universität, Zürich, Switzerland.
Piubelli
L
L
Haditsch
U
U
Bosshard
H R
HR
D000595:Amino Acid Sequence; D050976:Basic-Leucine Zipper Transcription Factors; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004058:Diffusion; D005656:Fungal Proteins / Q000378:metabolism; D051790:G-Box Binding Factors; D007700:Kinetics; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D011485:Protein Binding; D017510:Protein Folding; D011494:Protein Kinases / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D013050:Spectrometry, Fluorescence; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*
D050976:Basic-Leucine Zipper Transcription Factors; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D051790:G-Box Binding Factors; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D004247:DNA; D011494:Protein Kinases