Dimer-to-tetramer assembly of Lac repressor involves a leucine heptad repeat

S. Alberti, S. Oehler, B. Wilcken-Bergmann v., H. Kramer, B. Muller-Hill

Research output: Contribution to journalArticle

73 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)57-62
Number of pages6
JournalNew Biologist
Volume3
Issue number1
StatePublished - Apr 4 1991

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Alberti, S., Oehler, S., Wilcken-Bergmann v., B., Kramer, H., & Muller-Hill, B. (1991). Dimer-to-tetramer assembly of Lac repressor involves a leucine heptad repeat. New Biologist, 3(1), 57-62.