PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Picea abies
bZIP Family
Species TF ID Description
MA_101958g0010bZIP family protein
MA_103475g0010bZIP family protein
MA_10430819g0010bZIP family protein
MA_10431762g0010bZIP family protein
MA_10433986g0020bZIP family protein
MA_10435554g0020bZIP family protein
MA_105743g0010bZIP family protein
MA_110105g0020bZIP family protein
MA_11847g0020bZIP family protein
MA_127542g0020bZIP family protein
MA_130907g0010bZIP family protein
MA_132247g0010bZIP family protein
MA_139559g0010bZIP family protein
MA_142711g0010bZIP family protein
MA_155502g0010bZIP family protein
MA_161658g0010bZIP family protein
MA_162339g0010bZIP family protein
MA_170065g0010bZIP family protein
MA_18107g0010bZIP family protein
MA_19536g0010bZIP family protein
MA_19634g0010bZIP family protein
MA_19757g0010bZIP family protein
MA_23986g0010bZIP family protein
MA_28402g0010bZIP family protein
MA_297827g0010bZIP family protein
MA_30617g0010bZIP family protein
MA_33471g0010bZIP family protein
MA_35014g0010bZIP family protein
MA_367459g0010bZIP family protein
MA_38931g0010bZIP family protein
MA_3942g0010bZIP family protein
MA_41006g0010bZIP family protein
MA_59421g0010bZIP family protein
MA_61649g0010bZIP family protein
MA_6407g0010bZIP family protein
MA_757530g0010bZIP family protein
MA_7751g0010bZIP family protein
MA_91576g0010bZIP family protein
MA_9399348g0010bZIP family protein
MA_960494g0010bZIP 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