PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Marchantia polymorpha
bZIP Family
Species TF ID Description
Mapoly0001s0021.1.pbZIP family protein
Mapoly0007s0056.1.pbZIP family protein
Mapoly0012s0172.1.pbZIP family protein
Mapoly0015s0005.1.pbZIP family protein
Mapoly0016s0098.1.pbZIP family protein
Mapoly0016s0098.2.pbZIP family protein
Mapoly0019s0040.1.pbZIP family protein
Mapoly0019s0040.2.pbZIP family protein
Mapoly0022s0095.1.pbZIP family protein
Mapoly0022s0095.2.pbZIP family protein
Mapoly0026s0039.1.pbZIP family protein
Mapoly0026s0039.2.pbZIP family protein
Mapoly0026s0039.3.pbZIP family protein
Mapoly0026s0039.4.pbZIP family protein
Mapoly0026s0039.5.pbZIP family protein
Mapoly0026s0039.6.pbZIP family protein
Mapoly0026s0039.7.pbZIP family protein
Mapoly0026s0039.8.pbZIP family protein
Mapoly0034s0126.1.pbZIP family protein
Mapoly0046s0102.1.pbZIP family protein
Mapoly0069s0009.1.pbZIP family protein
Mapoly0072s0050.1.pbZIP family protein
Mapoly0072s0050.2.pbZIP family protein
Mapoly0130s0030.1.pbZIP family protein
Mapoly0130s0030.2.pbZIP family protein
Mapoly0130s0030.3.pbZIP family protein
Mapoly0737s0001.1.pbZIP family protein
bZIP Family Introduction

The bZIP domain consists of two structural features located on a contiguous alpha-helix: first, a basic region of ~ 16 amino acid residues containing a nuclear localization signal followed by an invariant N-x7-R/K motif that contacts the DNA; and, second, a heptad repeat of leucines or other bulky hydrophobic amino acids positioned exactly nine amino acids towards the C-terminus, creating an amphipathic helix. To bind DNA, two subunits adhere via interactions between the hydrophobic sides of their helices, which creates a superimposing coiled-coil structure. The ability to form homo- and heterodimers is influenced by the electrostatic attraction and repulsion of polar residues flanking the hydrophobic interaction surface of the helices.

Plant bZIP proteins preferentially bind to DNA sequences with an ACGT core. Binding specificity is regulated by flanking nucleotides. Plant bZIPs preferentially bind to the A-box (TACGTA), C-box (GACGTC) and G-box (CACGTG), but there are also examples of nonpalindromic binding sites.

Jakoby M, Weisshaar B, Droge-Laser W, Vicente-Carbajosa J, Tiedemann J, Kroj T, Parcy F
bZIP transcription factors in Arabidopsis.
Trends Plant Sci, 2002. 7(3): p. 106-11.
PMID: 11906833