Molecular recognition of bacterial phosphorelay proteins

Curr Opin Microbiol. 2002 Apr;5(2):142-8. doi: 10.1016/s1369-5274(02)00305-3.

Abstract

The transfer of the phosphoryl group from a histidine kinase to a response regulator forms the basis of bacterial signal transduction. The critical question of how a component of a signal transduction system specifically associates with its partner to produce the ideal environment for phosphotransfer is addressed in this review in the light of the structure of the Spo0F-Spo0B complex in Bacillus subtilis.

Publication types

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

MeSH terms

  • Bacillus subtilis / chemistry
  • Bacillus subtilis / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Models, Molecular
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphotransferases / chemistry*
  • Phosphotransferases / metabolism
  • Protein Binding
  • Protein Structure, Secondary
  • Response Elements
  • Sigma Factor*
  • Signal Transduction
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • Sigma Factor
  • Spo0F protein, Bacillus subtilis
  • Transcription Factors
  • spoIIR protein, Bacillus subtilis
  • spore-specific proteins, Bacillus
  • Phosphotransferases
  • Phosphoric Monoester Hydrolases