A universal target sequence is bound in vitro by diverse homeodomains

Mech Dev. 1993 Sep;43(1):57-70. doi: 10.1016/0925-4773(93)90023-q.

Abstract

To determine the number of DNA binding proteins capable of binding a consensus Engrailed binding site, this consensus sequence was used to screen a library of Drosophila cDNA clones in a bacteriophage expression vector. We retrieved clones encoding 20 distinct DNA binding domains, 17 of which are homeodomains. Binding to a variety of oligonucleotides confirms the related sequence specificity of the retrieved binding domains. Nonetheless, the homeodomains have remarkably diverse amino acid sequences. We conclude that during the evolutionary divergence of homeodomains, the specificity of DNA binding has been much more highly conserved than the amino acid sequence.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Consensus Sequence*
  • DNA, Complementary / genetics
  • DNA, Complementary / metabolism
  • DNA, Recombinant / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Drosophila Proteins
  • Drosophila melanogaster / embryology
  • Drosophila melanogaster / genetics*
  • Genes
  • Genes, Homeobox*
  • Genes, Insect
  • Homeodomain Proteins*
  • Insect Hormones / genetics
  • Insect Hormones / metabolism
  • Molecular Sequence Data
  • Multigene Family
  • Phylogeny
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Substrate Specificity
  • Transcription Factors / genetics
  • Transcription Factors / metabolism

Substances

  • DNA, Complementary
  • DNA, Recombinant
  • DNA-Binding Proteins
  • Drosophila Proteins
  • En protein, Drosophila
  • Homeodomain Proteins
  • Insect Hormones
  • Transcription Factors