Functional analyses of the Dof domain, a zinc finger DNA-binding domain, in a pumpkin DNA-binding protein AOBP.
AOBP, a DNA-binding protein in pumpkin, contains a Dof domain that is composed of 52 amino acid residues and is highly conserved in several DNA-binding proteins of higher plants. The Dof domain has a significant resemblance to Cys2/Cys2 zinc finger DNA-binding domains of steroid hormone receptors and GATA1, but has a longer putative loop where an extra Cys residue is conserved. We show that the Dof domain in AOBP functions as a zinc finger DNA-binding domain and suggest that the Cys residue uniquely conserved in the putative loop might negatively regulate the binding to DNA.
Faculty of Applied Biological Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima, Japan.
N
N
Shimofurutani
Y
Y
Kisu
M
M
Suzuki
M
M
Esaka
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D017124:Conserved Sequence; D019662:Cucurbitaceae / Q000235:genetics*; D003545:Cysteine; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins; D012091:Repetitive Sequences, Nucleic Acid; D016335:Zinc Fingers
D000596:Amino Acids; D004268:DNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D004247:DNA; D003545:Cysteine