Receiver domain structure and function in response regulator proteins

Curr Opin Microbiol. 2010 Apr;13(2):142-9. doi: 10.1016/j.mib.2010.01.015. Epub 2010 Mar 6.

Abstract

During signal transduction by two-component regulatory systems, sensor kinases detect and encode input information while response regulators (RRs) control output. Most receiver domains function as phosphorylation-mediated switches within RRs, but some transfer phosphoryl groups in multistep phosphorelays. Conserved features of receiver domain amino acid sequence correlate with structure and hence function. Receiver domains catalyze their own phosphorylation and dephosphorylation in reactions requiring a divalent cation. Molecular dynamics simulations are supplementing structural investigation of the conformational changes that underlie receiver domain switch function. As understanding of features shared by all receiver domains matures, factors conferring differences (e.g. in reaction rate or specificity) are receiving increased attention. Numerous examples of atypical receiver or pseudo-receiver domains that function without phosphorylation have recently been characterized.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Archaea / physiology
  • Archaeal Proteins* / chemistry
  • Archaeal Proteins* / genetics
  • Archaeal Proteins* / metabolism
  • Bacteria / growth & development
  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Gene Expression Regulation, Archaeal*
  • Gene Expression Regulation, Bacterial*
  • Phosphorylation
  • Signal Transduction*
  • Structure-Activity Relationship

Substances

  • Archaeal Proteins
  • Bacterial Proteins