CHASE: an extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants

Trends Biochem Sci. 2001 Oct;26(10):582-4. doi: 10.1016/s0968-0004(01)01969-7.


A novel extracellular ligand-binding domain, termed CHASE, is described in sensory adenylyl and diguanylate cyclases, and histidine kinases, in several bacterial species, Dictyostelium and plants. The CHASE domain is predicted to sense stimuli that are specific for the developmental program of an organism.

Publication types

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

MeSH terms

  • Adenylyl Cyclases / chemistry
  • Adenylyl Cyclases / genetics
  • Amino Acid Sequence
  • Animals
  • Eukaryotic Cells
  • Molecular Sequence Data
  • Plants / chemistry
  • Plants / genetics
  • Prokaryotic Cells
  • Protein Kinases / chemistry
  • Protein Kinases / genetics
  • Protein Structure, Tertiary
  • Protozoan Proteins*
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / genetics
  • Sequence Homology, Amino Acid


  • Protozoan Proteins
  • Receptors, Cell Surface
  • Protein Kinases
  • DhkA protein, Dictyostelium discoideum
  • ACG protein, Dictyostelium discoideum
  • Adenylyl Cyclases