The C-terminus of Lac repressor is responsible for the formation of repressor tetramers from active dimers. If properly grafted, the C-terminus of Lac repressor (amino acids 331 to 360) converts Gal repressor dimers into tetramers. Amino acids 342 to 356 of Lac repressor contain a 4-3 hydrophobic repeat of four leucines and one valine. Systematic amino acid replacements of all residues in this region show that the protein-protein interaction between repressor dimers depends mainly on the hydrophobic residues of the 4-3 repeat, which is constitutive for coiled coils. Thus the tetramerization site of Lac repressor resembles the leucine zipper motif found in a family of eukaryotic transcription factors.
|Original language||English (US)|
|Number of pages||6|
|State||Published - Apr 4 1991|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)