Interactions of coiled coils in transcription factors: where is the specificity?

Curr Opin Genet Dev. 1993 Apr;3(2):278-85. doi: 10.1016/0959-437x(93)90035-n.

Abstract

Amphipathic alpha-helices create the dimerization interface in the bZIP and bHLH classes of DNA-binding proteins. These amphipathic helices have been shown to enter into a wide variety of specific dimerization interactions, and this large array of possible combinatorial interactions may provide for fine control of biological function. In bHLH-ZIP proteins, the addition of a leucine-zipper region immediately carboxyl-terminal to the helix-loop-helix region provides for an additional level of both dimerization specificity and control, again through the interaction of amphipathic alpha-helices. Interhelical electrostatic interactions have been implicated in regulating dimerization specificity.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Basic-Leucine Zipper Transcription Factors
  • Chemical Phenomena
  • Chemistry, Physical
  • Consensus Sequence
  • DNA-Binding Proteins / chemistry*
  • Fungal Proteins / chemistry
  • G-Box Binding Factors
  • Leucine Zippers*
  • Models, Molecular
  • Molecular Sequence Data
  • Multigene Family
  • Plant Proteins / chemistry
  • Protein Binding
  • Protein Conformation*
  • Protein Kinases / chemistry
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Transcription Factors / chemistry*

Substances

  • Basic-Leucine Zipper Transcription Factors
  • DNA-Binding Proteins
  • Fungal Proteins
  • G-Box Binding Factors
  • Plant Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Protein Kinases