Determinants of T box protein specificity

Development. 2001 Oct;128(19):3749-58.

Abstract

Members of the T box family of transcription factors play important roles in early development. Different members of the family exert different effects and here we show that much of the specificity of the Xenopus T box proteins Xbra, VegT and Eomesodermin resides in the DNA-binding domain, or T box. Binding site selection experiments show that the three proteins bind the same core sequence, but they select paired sites that differ in their orientation and spacing. Lysine 149 of Xbra is conserved in all Brachyury homologues, while the corresponding amino acid in VegT and Eomesodermin is asparagine. Mutation of this amino acid to lysine changes the inductive abilities of VegT and Eomesodermin to resemble that of Xbra.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Asparagine / genetics
  • Binding Sites
  • Embryo, Nonmammalian
  • Female
  • Fetal Proteins*
  • Gene Expression Regulation, Developmental*
  • Lysine / genetics
  • Molecular Sequence Data
  • Point Mutation
  • Repetitive Sequences, Nucleic Acid
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • T-Box Domain Proteins / genetics*
  • T-Box Domain Proteins / metabolism*
  • Xenopus / embryology
  • Xenopus / genetics
  • Xenopus Proteins*

Substances

  • EOMES protein, Xenopus
  • Fetal Proteins
  • T-Box Domain Proteins
  • TBXT protein, Xenopus
  • VegT protein, Xenopus
  • Xenopus Proteins
  • Asparagine
  • Brachyury protein
  • Lysine