PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Arabis alpina
bZIP Family
Species TF ID Description
KFK22532.1bZIP family protein
KFK22898.1bZIP family protein
KFK25074.1bZIP family protein
KFK25075.1bZIP family protein
KFK25109.1bZIP family protein
KFK25110.1bZIP family protein
KFK25396.1bZIP family protein
KFK26588.1bZIP family protein
KFK27095.1bZIP family protein
KFK27703.1bZIP family protein
KFK27745.1bZIP family protein
KFK27808.1bZIP family protein
KFK30089.1bZIP family protein
KFK30142.1bZIP family protein
KFK30225.1bZIP family protein
KFK30382.1bZIP family protein
KFK30861.1bZIP family protein
KFK31667.1bZIP family protein
KFK31772.1bZIP family protein
KFK31935.1bZIP family protein
KFK34127.1bZIP family protein
KFK34704.1bZIP family protein
KFK34907.1bZIP family protein
KFK34922.1bZIP family protein
KFK35037.1bZIP family protein
KFK35422.1bZIP family protein
KFK36518.1bZIP family protein
KFK36932.1bZIP family protein
KFK37054.1bZIP family protein
KFK38471.1bZIP family protein
KFK39090.1bZIP family protein
KFK39850.1bZIP family protein
KFK40204.1bZIP family protein
KFK41287.1bZIP family protein
KFK41324.1bZIP family protein
KFK41975.1bZIP family protein
KFK42323.1bZIP family protein
KFK42741.1bZIP family protein
KFK42999.1bZIP family protein
KFK43613.1bZIP family protein
KFK44082.1bZIP 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