PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Dioscorea rotundata
bZIP Family
Species TF ID Description
Dr00703.1bZIP family protein
Dr01024.1bZIP family protein
Dr01663.1bZIP family protein
Dr02084.1bZIP family protein
Dr02965.1bZIP family protein
Dr03422.1bZIP family protein
Dr03502.1bZIP family protein
Dr03731.1bZIP family protein
Dr04536.1bZIP family protein
Dr04911.1bZIP family protein
Dr05218.1bZIP family protein
Dr06251.1bZIP family protein
Dr06308.1bZIP family protein
Dr06741.1bZIP family protein
Dr07236.1bZIP family protein
Dr07346.1bZIP family protein
Dr07485.1bZIP family protein
Dr07918.1bZIP family protein
Dr08502.1bZIP family protein
Dr08987.1bZIP family protein
Dr09143.1bZIP family protein
Dr09470.1bZIP family protein
Dr09627.1bZIP family protein
Dr10825.1bZIP family protein
Dr12037.1bZIP family protein
Dr13430.1bZIP family protein
Dr13627.1bZIP family protein
Dr13719.1bZIP family protein
Dr13961.1bZIP family protein
Dr14202.1bZIP family protein
Dr14951.1bZIP family protein
Dr15659.1bZIP family protein
Dr16911.1bZIP family protein
Dr17141.1bZIP family protein
Dr18364.1bZIP family protein
Dr18675.1bZIP family protein
Dr19019.1bZIP family protein
Dr21106.1bZIP 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