PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Saccharum officinarum
bZIP Family
Species TF ID Description
Sof000283bZIP family protein
Sof000727bZIP family protein
Sof001897bZIP family protein
Sof002037bZIP family protein
Sof002067bZIP family protein
Sof002483bZIP family protein
Sof002535bZIP family protein
Sof002819bZIP family protein
Sof004384bZIP family protein
Sof006584bZIP family protein
Sof008078bZIP family protein
Sof008184bZIP family protein
Sof008245bZIP family protein
Sof008596bZIP family protein
Sof008937bZIP family protein
Sof009733bZIP family protein
Sof010189bZIP family protein
Sof011056bZIP family protein
Sof011876bZIP family protein
Sof012274bZIP family protein
Sof013743bZIP family protein
Sof013951bZIP family protein
Sof014422bZIP family protein
Sof014687bZIP family protein
Sof015384bZIP family protein
Sof015728bZIP family protein
Sof015874bZIP family protein
Sof016074bZIP family protein
Sof016918bZIP family protein
Sof017283bZIP family protein
Sof018703bZIP family protein
Sof018704bZIP family protein
Sof018800bZIP family protein
Sof019132bZIP family protein
Sof019189bZIP family protein
Sof019222bZIP family protein
Sof019846bZIP 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