PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Morus notabilis
bZIP Family
Species TF ID Description
XP_010086697.1bZIP family protein
XP_010087124.1bZIP family protein
XP_010087242.1bZIP family protein
XP_010087331.1bZIP family protein
XP_010088657.1bZIP family protein
XP_010089523.1bZIP family protein
XP_010089829.1bZIP family protein
XP_010089831.1bZIP family protein
XP_010091673.1bZIP family protein
XP_010092905.1bZIP family protein
XP_010093582.1bZIP family protein
XP_010093801.1bZIP family protein
XP_010094499.1bZIP family protein
XP_010095553.1bZIP family protein
XP_010095678.1bZIP family protein
XP_010095986.1bZIP family protein
XP_010096209.1bZIP family protein
XP_010098424.1bZIP family protein
XP_010099501.1bZIP family protein
XP_010099832.1bZIP family protein
XP_010099919.1bZIP family protein
XP_010100890.1bZIP family protein
XP_010101577.1bZIP family protein
XP_010102841.1bZIP family protein
XP_010103645.1bZIP family protein
XP_010103855.1bZIP family protein
XP_010104020.1bZIP family protein
XP_010105000.1bZIP family protein
XP_010105258.1bZIP family protein
XP_010105351.1bZIP family protein
XP_010105854.1bZIP family protein
XP_010105855.1bZIP family protein
XP_010106904.1bZIP family protein
XP_010107666.1bZIP family protein
XP_010107932.1bZIP family protein
XP_010108472.1bZIP family protein
XP_010108629.1bZIP family protein
XP_010108652.1bZIP family protein
XP_010109918.1bZIP family protein
XP_010110029.1bZIP family protein
XP_010110125.1bZIP family protein
XP_010110356.1bZIP family protein
XP_010110596.1bZIP family protein
XP_010111098.1bZIP family protein
XP_010111311.1bZIP family protein
XP_010111398.1bZIP family protein
XP_010112149.1bZIP family protein
XP_010112189.1bZIP family protein
XP_010113175.1bZIP family protein
XP_010113304.1bZIP 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