Functional analyses of the Dof domain, a zinc finger DNA-binding domain, in a pumpkin DNA-binding protein AOBP

FEBS Lett. 1998 Jul 3;430(3):251-6. doi: 10.1016/s0014-5793(98)00670-x.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / metabolism
  • Conserved Sequence
  • Cucurbitaceae / genetics*
  • Cysteine
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Molecular Sequence Data
  • Mutation
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Repetitive Sequences, Nucleic Acid
  • Zinc Fingers*

Substances

  • Amino Acids
  • DNA-Binding Proteins
  • Recombinant Fusion Proteins
  • DNA
  • Cysteine

Associated data

  • GENBANK/D45066