Sensory transducers of E. coli are composed of discrete structural and functional domains

Cell. 1983 Jun;33(2):615-22. doi: 10.1016/0092-8674(83)90442-7.


The tar and tsr genes of E. coli encode functionally analogous transducer proteins that mediate two distinct classes of chemotactic response. The tap gene lies adjacent to tar, and is thought to encode another transducer protein. We present here the complete nucleotide sequence of the tar-tap region of the E. coli genome, together with a comparative analysis of the sequences of the Tar, Tap, and Tsr proteins. The proteins appear to have a simple transmembrane structure consisting of an extracytoplasmic amino-terminal domain, a membrane-spanning domain, and an intracellular carboxy-terminal domain. The carboxy-terminal domains of three proteins possess highly homologous sequences and contain sites of methylation involved in sensory adaptation, while the amino-terminal sequences are only distantly related to one another, consistent with their serving as chemoreceptor domains that have diverged functionally.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / analysis
  • Base Sequence
  • Escherichia coli / genetics
  • Genes, Bacterial*
  • Methylation
  • Transduction, Genetic*


  • Bacterial Proteins

Associated data

  • GENBANK/J01705